TY  - JOUR
AU  - Čolović, Mirjana B.
AU  - Krstić, Danijela Z.
AU  - Krinulović, Katarina
AU  - Momić, Tatjana
AU  - Savić, Jasmina
AU  - Vujačić, Ana V.
AU  - Vasić, Vesna M.
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/6815
AB  - The aim of the study was to give an overview of the mechanism of inhibition of Na+/K+-ATPase activity induced by some specific and non specific inhibitors. For this purpose, the effects of some ouabain like compounds (digoxin, gitoxin), noble metals complexes ([PtCl2DMSO2], [AuCl4](-), [PdCl4](2-), [PdCl(dien)](+), [PdCl(Me(4)dien)](+)), transition metal ions (Cu2+, Zn2+, Fe2+, Co2+), and heavy metal ions (Hg2+, Pb2+, Cd2+) on the activity of Na+/K+-ATPase from rat synaptic plasma membranes (SPM), porcine cerebral cortex and human erythrocytes were discussed.
T2  - Russian Journal of Physical Chemistry A
T1  - Na+/K+-ATPase: Activity and inhibition
VL  - 83
IS  - 9
SP  - 1602
EP  - 1608
DO  - 10.1134/S0036024409090337
ER  - 

@article{
author = "Čolović, Mirjana B. and Krstić, Danijela Z. and Krinulović, Katarina and Momić, Tatjana and Savić, Jasmina and Vujačić, Ana V. and Vasić, Vesna M.",
year = "2009",
abstract = "The aim of the study was to give an overview of the mechanism of inhibition of Na+/K+-ATPase activity induced by some specific and non specific inhibitors. For this purpose, the effects of some ouabain like compounds (digoxin, gitoxin), noble metals complexes ([PtCl2DMSO2], [AuCl4](-), [PdCl4](2-), [PdCl(dien)](+), [PdCl(Me(4)dien)](+)), transition metal ions (Cu2+, Zn2+, Fe2+, Co2+), and heavy metal ions (Hg2+, Pb2+, Cd2+) on the activity of Na+/K+-ATPase from rat synaptic plasma membranes (SPM), porcine cerebral cortex and human erythrocytes were discussed.",
journal = "Russian Journal of Physical Chemistry A",
title = "Na+/K+-ATPase: Activity and inhibition",
volume = "83",
number = "9",
pages = "1602-1608",
doi = "10.1134/S0036024409090337"
}

Čolović, M. B., Krstić, D. Z., Krinulović, K., Momić, T., Savić, J., Vujačić, A. V.,& Vasić, V. M.. (2009). Na+/K+-ATPase: Activity and inhibition. in Russian Journal of Physical Chemistry A, 83(9), 1602-1608.
https://doi.org/10.1134/S0036024409090337

Čolović MB, Krstić DZ, Krinulović K, Momić T, Savić J, Vujačić AV, Vasić VM. Na+/K+-ATPase: Activity and inhibition. in Russian Journal of Physical Chemistry A. 2009;83(9):1602-1608.
doi:10.1134/S0036024409090337 .

Čolović, Mirjana B., Krstić, Danijela Z., Krinulović, Katarina, Momić, Tatjana, Savić, Jasmina, Vujačić, Ana V., Vasić, Vesna M., "Na+/K+-ATPase: Activity and inhibition" in Russian Journal of Physical Chemistry A, 83, no. 9 (2009):1602-1608,
https://doi.org/10.1134/S0036024409090337 . .

TY  - CONF
AU  - Savić, Jasmina
AU  - Krinulović, Katarina
AU  - Momić, Tatjana
AU  - Čolović, Mirjana B.
AU  - Vujačić, Ana V.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9354
AB  - An ion-pair ultra performance liquid chromatography (IP-UPLC) method was developed to obtain a sensitive and efficient means for quantification of ADP in order to follow the decrease of Na+ /K+  ATPase activity after its exposure to different inhibitors. The concentrations of ADP obtained after hydrolysis of ATP in the presence of enzyme depends on enzyme activity. Simultaneously with the chromatographic determination of ADP, the spectrophotometric determination of phosphates liberated after the hydrolysis of ATP was done.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
T1  - Application of ultra performance liquid chromatography (uplc) for determination of Na+ /K+ atpase activity
VL  - 1
SP  - 36
EP  - 38
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9354
ER  - 

@conference{
author = "Savić, Jasmina and Krinulović, Katarina and Momić, Tatjana and Čolović, Mirjana B. and Vujačić, Ana V.",
year = "2008",
abstract = "An ion-pair ultra performance liquid chromatography (IP-UPLC) method was developed to obtain a sensitive and efficient means for quantification of ADP in order to follow the decrease of Na+ /K+  ATPase activity after its exposure to different inhibitors. The concentrations of ADP obtained after hydrolysis of ATP in the presence of enzyme depends on enzyme activity. Simultaneously with the chromatographic determination of ADP, the spectrophotometric determination of phosphates liberated after the hydrolysis of ATP was done.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry",
title = "Application of ultra performance liquid chromatography (uplc) for determination of Na+ /K+ atpase activity",
volume = "1",
pages = "36-38",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9354"
}

Savić, J., Krinulović, K., Momić, T., Čolović, M. B.,& Vujačić, A. V.. (2008). Application of ultra performance liquid chromatography (uplc) for determination of Na+ /K+ atpase activity. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia., 1, 36-38.
https://hdl.handle.net/21.15107/rcub_vinar_9354

Savić J, Krinulović K, Momić T, Čolović MB, Vujačić AV. Application of ultra performance liquid chromatography (uplc) for determination of Na+ /K+ atpase activity. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry. 2008;1:36-38.
https://hdl.handle.net/21.15107/rcub_vinar_9354 .

Savić, Jasmina, Krinulović, Katarina, Momić, Tatjana, Čolović, Mirjana B., Vujačić, Ana V., "Application of ultra performance liquid chromatography (uplc) for determination of Na+ /K+ atpase activity" in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry, 1 (2008):36-38,
https://hdl.handle.net/21.15107/rcub_vinar_9354 .

TY  - JOUR
AU  - Krstić, Danijela Z.
AU  - Čolović, Mirjana B.
AU  - Kralj, Mojca Bavcon
AU  - Franko, Mladen
AU  - Krinulović, Katarina
AU  - Trebše, Polonca
AU  - Vasić, Vesna M.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3499
AB  - Inhibition of bovine erythrocyte acetylcholinesterase (free and immobilized on controlled pore glass) by separate and simultaneous exposure to malathion and malathion transformation products which are generally formed during storage or through natural or photochemical degradation was investigated. Increasing concentrations of malathion, its oxidation product malaoxon, and its isomerisation product isomalathion inhibited free and immobilized AChE in a concentration-dependent manner. K-I, the dissociation constant for the initial reversible enzyme inhibitor-complex, and k(3), the first order rate constant for the conversion of the reversible complex into the irreversibly inhibited enzyme, were determined from the progressive development of inhibition produced by reaction of native AChE with malathion, malaoxon and isomalathion. KI values of 1.3 x 10(-4) M-1, 5.6 x 10(-6) M-1 and 7.2 x 10(-6) M-1 were obtained for malathion, malaoxon and isomalathion, respectively. The IC50 values for free/immobilized AChE, (3.7 +/- 0.2)10(-4) M/(1.6 +/- 0.1)10(-4), (2.4 +/- 0.3)10(-6)/(3.4 +/- 0.1)10(-6) M and (3.2 +/- 0.3)10(-6) M/(2.7 +/- 0.2)10(-6) M, were obtained from the inhibition curves induced by malathion, malaoxon and isomalathion, respectively. However, the products formed due to photoinduced degradation, phosphorodithioic O,O,S-trimethyl ester and O,O-dimethyl thiophosphate, did not noticeably affect enzymatic activity, while diethyl maleate inhibited AChE activity at concentrations GT 10 mM. Inhibition of acetylcholinesterase increased with the time of exposure to malathion and its inhibiting by-products within the interval from 0 to 5 minutes. Through simultaneous exposure of the enzyme to malaoxon and isomalathion, an additive effect was achieved for lower concentrations of the inhibitors (in the presence of malaoxon/isomalathion at concentrations 2 x 10(-7) M/2 x 10(-7) M, 2 x 10(-7) M/3 x 10(-7) M and 2 x 10(-7) M/4.5 x 10(-7)M), while an antagonistic effect was obtained for all higher concentrations of inhibitors. The presence of a non-inhibitory degradation product (phosphorodithioic O,O,S-trimethyl ester) did not affect the inhibition efficiencies of the malathion by-products, malaoxon and isomalathion.
T2  - Journal of Enzyme Inhibition and Medicinal Chemistry
T1  - Inhibition of AChE by malathion and some structurally similar compounds
VL  - 23
IS  - 4
SP  - 562
EP  - 573
DO  - 10.1080/14756360701632031
ER  - 

@article{
author = "Krstić, Danijela Z. and Čolović, Mirjana B. and Kralj, Mojca Bavcon and Franko, Mladen and Krinulović, Katarina and Trebše, Polonca and Vasić, Vesna M.",
year = "2008",
abstract = "Inhibition of bovine erythrocyte acetylcholinesterase (free and immobilized on controlled pore glass) by separate and simultaneous exposure to malathion and malathion transformation products which are generally formed during storage or through natural or photochemical degradation was investigated. Increasing concentrations of malathion, its oxidation product malaoxon, and its isomerisation product isomalathion inhibited free and immobilized AChE in a concentration-dependent manner. K-I, the dissociation constant for the initial reversible enzyme inhibitor-complex, and k(3), the first order rate constant for the conversion of the reversible complex into the irreversibly inhibited enzyme, were determined from the progressive development of inhibition produced by reaction of native AChE with malathion, malaoxon and isomalathion. KI values of 1.3 x 10(-4) M-1, 5.6 x 10(-6) M-1 and 7.2 x 10(-6) M-1 were obtained for malathion, malaoxon and isomalathion, respectively. The IC50 values for free/immobilized AChE, (3.7 +/- 0.2)10(-4) M/(1.6 +/- 0.1)10(-4), (2.4 +/- 0.3)10(-6)/(3.4 +/- 0.1)10(-6) M and (3.2 +/- 0.3)10(-6) M/(2.7 +/- 0.2)10(-6) M, were obtained from the inhibition curves induced by malathion, malaoxon and isomalathion, respectively. However, the products formed due to photoinduced degradation, phosphorodithioic O,O,S-trimethyl ester and O,O-dimethyl thiophosphate, did not noticeably affect enzymatic activity, while diethyl maleate inhibited AChE activity at concentrations GT 10 mM. Inhibition of acetylcholinesterase increased with the time of exposure to malathion and its inhibiting by-products within the interval from 0 to 5 minutes. Through simultaneous exposure of the enzyme to malaoxon and isomalathion, an additive effect was achieved for lower concentrations of the inhibitors (in the presence of malaoxon/isomalathion at concentrations 2 x 10(-7) M/2 x 10(-7) M, 2 x 10(-7) M/3 x 10(-7) M and 2 x 10(-7) M/4.5 x 10(-7)M), while an antagonistic effect was obtained for all higher concentrations of inhibitors. The presence of a non-inhibitory degradation product (phosphorodithioic O,O,S-trimethyl ester) did not affect the inhibition efficiencies of the malathion by-products, malaoxon and isomalathion.",
journal = "Journal of Enzyme Inhibition and Medicinal Chemistry",
title = "Inhibition of AChE by malathion and some structurally similar compounds",
volume = "23",
number = "4",
pages = "562-573",
doi = "10.1080/14756360701632031"
}

Krstić, D. Z., Čolović, M. B., Kralj, M. B., Franko, M., Krinulović, K., Trebše, P.,& Vasić, V. M.. (2008). Inhibition of AChE by malathion and some structurally similar compounds. in Journal of Enzyme Inhibition and Medicinal Chemistry, 23(4), 562-573.
https://doi.org/10.1080/14756360701632031

Krstić DZ, Čolović MB, Kralj MB, Franko M, Krinulović K, Trebše P, Vasić VM. Inhibition of AChE by malathion and some structurally similar compounds. in Journal of Enzyme Inhibition and Medicinal Chemistry. 2008;23(4):562-573.
doi:10.1080/14756360701632031 .

Krstić, Danijela Z., Čolović, Mirjana B., Kralj, Mojca Bavcon, Franko, Mladen, Krinulović, Katarina, Trebše, Polonca, Vasić, Vesna M., "Inhibition of AChE by malathion and some structurally similar compounds" in Journal of Enzyme Inhibition and Medicinal Chemistry, 23, no. 4 (2008):562-573,
https://doi.org/10.1080/14756360701632031 . .

TY  - JOUR
AU  - Krstić, Danijela Z.
AU  - Čolović, Mirjana B.
AU  - Kralj, M. B.
AU  - Trebše, Polonca
AU  - Krinulović, Katarina
AU  - Vasić, Vesna M.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3421
AB  - The influence of malathion and its four main degradation products found in irradiated solutions (malaoxon, isomalathion, diethyl maleate and O,O-dimethyl phosphate) on acetylcholinesterase (AChE) of free and immobilized bovine erythrocytes was investigated. The concentration-dependent responses to malathion and related organophosphates, malaoxon and isomalathion, of both AChE bioassays used were obtained. The IC (50) values for free and immobilized AChE (3.7 +/- 0.2) x 10(-4) M/(1.6 +/- 0.1) x 10(-4), (2.4 +/- 0.3) x 10(-6)/(3.4 +/- 0.1) x 10(-6) M, and (3.2 +/- 0.3) x 10(-6) M/(2.7 +/- 0.2) x 10(-6) M were obtained in the presence of malathion, malaoxon and isomalathion, respectively. However, diethyl maleate inhibited AChE activity at concentrations GT = 10 mM, while O,O-dimethyl phosphate did not noticeably affect enzyme activity at all investigated concentrations. The relation between the structure of the compounds and their ability to inhibit enzyme activity was discussed.
T2  - Russian Journal of Physical Chemistry A
T1  - The influence of malathion and its decomposition products on free and immobilized acetylcholinesterase
VL  - 82
IS  - 4
SP  - 663
EP  - 668
DO  - 10.1134/S0036024408040274
ER  - 

@article{
author = "Krstić, Danijela Z. and Čolović, Mirjana B. and Kralj, M. B. and Trebše, Polonca and Krinulović, Katarina and Vasić, Vesna M.",
year = "2008",
abstract = "The influence of malathion and its four main degradation products found in irradiated solutions (malaoxon, isomalathion, diethyl maleate and O,O-dimethyl phosphate) on acetylcholinesterase (AChE) of free and immobilized bovine erythrocytes was investigated. The concentration-dependent responses to malathion and related organophosphates, malaoxon and isomalathion, of both AChE bioassays used were obtained. The IC (50) values for free and immobilized AChE (3.7 +/- 0.2) x 10(-4) M/(1.6 +/- 0.1) x 10(-4), (2.4 +/- 0.3) x 10(-6)/(3.4 +/- 0.1) x 10(-6) M, and (3.2 +/- 0.3) x 10(-6) M/(2.7 +/- 0.2) x 10(-6) M were obtained in the presence of malathion, malaoxon and isomalathion, respectively. However, diethyl maleate inhibited AChE activity at concentrations GT = 10 mM, while O,O-dimethyl phosphate did not noticeably affect enzyme activity at all investigated concentrations. The relation between the structure of the compounds and their ability to inhibit enzyme activity was discussed.",
journal = "Russian Journal of Physical Chemistry A",
title = "The influence of malathion and its decomposition products on free and immobilized acetylcholinesterase",
volume = "82",
number = "4",
pages = "663-668",
doi = "10.1134/S0036024408040274"
}

Krstić, D. Z., Čolović, M. B., Kralj, M. B., Trebše, P., Krinulović, K.,& Vasić, V. M.. (2008). The influence of malathion and its decomposition products on free and immobilized acetylcholinesterase. in Russian Journal of Physical Chemistry A, 82(4), 663-668.
https://doi.org/10.1134/S0036024408040274

Krstić DZ, Čolović MB, Kralj MB, Trebše P, Krinulović K, Vasić VM. The influence of malathion and its decomposition products on free and immobilized acetylcholinesterase. in Russian Journal of Physical Chemistry A. 2008;82(4):663-668.
doi:10.1134/S0036024408040274 .

Krstić, Danijela Z., Čolović, Mirjana B., Kralj, M. B., Trebše, Polonca, Krinulović, Katarina, Vasić, Vesna M., "The influence of malathion and its decomposition products on free and immobilized acetylcholinesterase" in Russian Journal of Physical Chemistry A, 82, no. 4 (2008):663-668,
https://doi.org/10.1134/S0036024408040274 . .

TY  - JOUR
AU  - Vasić, Vesna M.
AU  - Krinulović, Katarina
AU  - Momić, Tatjana
AU  - Čolović, Mirjana B.
AU  - Vujačić, Ana V.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3550
AB  - The influence of some organic compounds (pyridine, urea, chlorpyrifos, permethrin) and metal ions (Pb2+, Cd2-, Hg2+, Cu2+, Fe2+ and Zn2+) on Na+/K+-ATPase and Mg2+-ATpase activity isolated from rat brain synaptic plasma membranes (SPM) was investigated in order to develop a simple semi-quantitative and qualitative test method for selective detection of these analyites in aqueous solutions. The method is based on the spectrophotometric determination of inorganic ortho-phosphate (P-i) that serves as a measure of the enzymatic activity in the presence of various analytes. The concentration of P-p liberated by enzyme-catalysed hydrolysis of adenosinetriphosphate (ATP), by exposure to analytes was dose-dependent on the analyte concentration. Heavy metals (Pb, Cd, Hg, Cu, Fe and Zn), toxic organic compounds (pyridine, urea) and some pesticides (ehlorpyrifos, permethrin) showed diverse effects, inducing the inhibition or stimulation of the enzyme activity. Development of simple test method for simultaneous detection of the investigated analytes based on the variation of medium assay composition was discussed.
T2  - Journal of Environmental Protection and Ecology
T1  - Effects of Some Organic and Inorganic Compounds on Atpase Activity
VL  - 9
IS  - 3
SP  - 583
EP  - 591
UR  - https://hdl.handle.net/21.15107/rcub_vinar_3550
ER  - 

@article{
author = "Vasić, Vesna M. and Krinulović, Katarina and Momić, Tatjana and Čolović, Mirjana B. and Vujačić, Ana V.",
year = "2008",
abstract = "The influence of some organic compounds (pyridine, urea, chlorpyrifos, permethrin) and metal ions (Pb2+, Cd2-, Hg2+, Cu2+, Fe2+ and Zn2+) on Na+/K+-ATPase and Mg2+-ATpase activity isolated from rat brain synaptic plasma membranes (SPM) was investigated in order to develop a simple semi-quantitative and qualitative test method for selective detection of these analyites in aqueous solutions. The method is based on the spectrophotometric determination of inorganic ortho-phosphate (P-i) that serves as a measure of the enzymatic activity in the presence of various analytes. The concentration of P-p liberated by enzyme-catalysed hydrolysis of adenosinetriphosphate (ATP), by exposure to analytes was dose-dependent on the analyte concentration. Heavy metals (Pb, Cd, Hg, Cu, Fe and Zn), toxic organic compounds (pyridine, urea) and some pesticides (ehlorpyrifos, permethrin) showed diverse effects, inducing the inhibition or stimulation of the enzyme activity. Development of simple test method for simultaneous detection of the investigated analytes based on the variation of medium assay composition was discussed.",
journal = "Journal of Environmental Protection and Ecology",
title = "Effects of Some Organic and Inorganic Compounds on Atpase Activity",
volume = "9",
number = "3",
pages = "583-591",
url = "https://hdl.handle.net/21.15107/rcub_vinar_3550"
}

Vasić, V. M., Krinulović, K., Momić, T., Čolović, M. B.,& Vujačić, A. V.. (2008). Effects of Some Organic and Inorganic Compounds on Atpase Activity. in Journal of Environmental Protection and Ecology, 9(3), 583-591.
https://hdl.handle.net/21.15107/rcub_vinar_3550

Vasić VM, Krinulović K, Momić T, Čolović MB, Vujačić AV. Effects of Some Organic and Inorganic Compounds on Atpase Activity. in Journal of Environmental Protection and Ecology. 2008;9(3):583-591.
https://hdl.handle.net/21.15107/rcub_vinar_3550 .

Vasić, Vesna M., Krinulović, Katarina, Momić, Tatjana, Čolović, Mirjana B., Vujačić, Ana V., "Effects of Some Organic and Inorganic Compounds on Atpase Activity" in Journal of Environmental Protection and Ecology, 9, no. 3 (2008):583-591,
https://hdl.handle.net/21.15107/rcub_vinar_3550 .

TY  - JOUR
AU  - Pavelkić, Vesna M.
AU  - Krinulović, Katarina
AU  - Savić, Jasmina
AU  - Ilic, M. A.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3444
AB  - The in vitro effect of technical grade malathion was assessed via the kinetic parameters of human plasma butyrylcholinesterase (BChE) using N-methylindoxyl acetate as a substrate for BChE. An inhibitor kinetics study demonstrated the existence of a biphasic inhibition curve, indicating high-and low-affinity binding sites of malathion. The IC (50) values as calculated from the experimental inhibition curves were 1.33 x 10(-9) and 1.48 x 10(-5) M for the high-and low-affinity binding sites, respectively; Hills analysis gave 1.29 x 10(-9) and 1.38 x 10(-6) M. The Cornish-Bowden plots and their secondary plots indicated that the nature of inhibition was of mixed type with the predominant competitive character of both affinity binding sites.
T2  - Russian Journal of Physical Chemistry A
T1  - Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method
VL  - 82
IS  - 5
SP  - 870
EP  - 874
DO  - 10.1134/S0036024408050312
ER  - 

@article{
author = "Pavelkić, Vesna M. and Krinulović, Katarina and Savić, Jasmina and Ilic, M. A.",
year = "2008",
abstract = "The in vitro effect of technical grade malathion was assessed via the kinetic parameters of human plasma butyrylcholinesterase (BChE) using N-methylindoxyl acetate as a substrate for BChE. An inhibitor kinetics study demonstrated the existence of a biphasic inhibition curve, indicating high-and low-affinity binding sites of malathion. The IC (50) values as calculated from the experimental inhibition curves were 1.33 x 10(-9) and 1.48 x 10(-5) M for the high-and low-affinity binding sites, respectively; Hills analysis gave 1.29 x 10(-9) and 1.38 x 10(-6) M. The Cornish-Bowden plots and their secondary plots indicated that the nature of inhibition was of mixed type with the predominant competitive character of both affinity binding sites.",
journal = "Russian Journal of Physical Chemistry A",
title = "Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method",
volume = "82",
number = "5",
pages = "870-874",
doi = "10.1134/S0036024408050312"
}

Pavelkić, V. M., Krinulović, K., Savić, J.,& Ilic, M. A.. (2008). Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method. in Russian Journal of Physical Chemistry A, 82(5), 870-874.
https://doi.org/10.1134/S0036024408050312

Pavelkić VM, Krinulović K, Savić J, Ilic MA. Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method. in Russian Journal of Physical Chemistry A. 2008;82(5):870-874.
doi:10.1134/S0036024408050312 .

Pavelkić, Vesna M., Krinulović, Katarina, Savić, Jasmina, Ilic, M. A., "Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method" in Russian Journal of Physical Chemistry A, 82, no. 5 (2008):870-874,
https://doi.org/10.1134/S0036024408050312 . .

TY  - JOUR
AU  - Vasić, Vesna M.
AU  - Kojić, Dušan
AU  - Krinulović, Katarina
AU  - Čolović, Mirjana B.
AU  - Vujačić, Ana V.
AU  - Stojić, Dragica Lj.
PY  - 2007
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/6719
AB  - Time-dependent interactions of Na+/K+-ATPase, isolated from rat brain synaptic plasma membranes (SPMs), with Cd2+ and Pb2+ ions in a single exposure and in a mixture were investigated in vitro. The interference of the enzyme with these metal ions was studied as a function of different protein concentrations and exposure time. The aim of the work was to investigate the possibility of selective recognition of Cd2+ and Pb2+ ions in a mixture, on the basis of the different rates of their protein-ligand interactions. Decreasing protein concentration increased the sensitivity of Na+/K+-ATPase toward both metals. The selectivity in protein-ligand interactions was obtained by variation of preincubation time (incubation before starting the enzymatic reaction).
T2  - Russian Journal of Physical Chemistry A
T1  - Time-dependent inhibition of Na+/K+-ATPase induced by single and simultaneous exposure to lead and cadmium
VL  - 81
IS  - 9
SP  - 1402
EP  - 1406
DO  - 10.1134/S0036024407090105
ER  - 

@article{
author = "Vasić, Vesna M. and Kojić, Dušan and Krinulović, Katarina and Čolović, Mirjana B. and Vujačić, Ana V. and Stojić, Dragica Lj.",
year = "2007",
abstract = "Time-dependent interactions of Na+/K+-ATPase, isolated from rat brain synaptic plasma membranes (SPMs), with Cd2+ and Pb2+ ions in a single exposure and in a mixture were investigated in vitro. The interference of the enzyme with these metal ions was studied as a function of different protein concentrations and exposure time. The aim of the work was to investigate the possibility of selective recognition of Cd2+ and Pb2+ ions in a mixture, on the basis of the different rates of their protein-ligand interactions. Decreasing protein concentration increased the sensitivity of Na+/K+-ATPase toward both metals. The selectivity in protein-ligand interactions was obtained by variation of preincubation time (incubation before starting the enzymatic reaction).",
journal = "Russian Journal of Physical Chemistry A",
title = "Time-dependent inhibition of Na+/K+-ATPase induced by single and simultaneous exposure to lead and cadmium",
volume = "81",
number = "9",
pages = "1402-1406",
doi = "10.1134/S0036024407090105"
}

Vasić, V. M., Kojić, D., Krinulović, K., Čolović, M. B., Vujačić, A. V.,& Stojić, D. Lj.. (2007). Time-dependent inhibition of Na+/K+-ATPase induced by single and simultaneous exposure to lead and cadmium. in Russian Journal of Physical Chemistry A, 81(9), 1402-1406.
https://doi.org/10.1134/S0036024407090105

Vasić VM, Kojić D, Krinulović K, Čolović MB, Vujačić AV, Stojić DL. Time-dependent inhibition of Na+/K+-ATPase induced by single and simultaneous exposure to lead and cadmium. in Russian Journal of Physical Chemistry A. 2007;81(9):1402-1406.
doi:10.1134/S0036024407090105 .

Vasić, Vesna M., Kojić, Dušan, Krinulović, Katarina, Čolović, Mirjana B., Vujačić, Ana V., Stojić, Dragica Lj., "Time-dependent inhibition of Na+/K+-ATPase induced by single and simultaneous exposure to lead and cadmium" in Russian Journal of Physical Chemistry A, 81, no. 9 (2007):1402-1406,
https://doi.org/10.1134/S0036024407090105 . .

TY  - JOUR
AU  - Krstić, Danijela Z.
AU  - Čolović, Mirjana B.
AU  - Krinulović, Katarina
AU  - Đurić, Dragan M.
AU  - Vasić, Vesna M.
PY  - 2007
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3364
AB  - In vitro inhibition of bovine erythrocytes acetylcholinesterase (AchE) by separate and simultaneous exposure to organophosphorous insecticide malathion and the transformation products, which are generally formed during the storage or natural as well as photochemical degradation pathways of malathion, was investigated. The increasing concentration of malathion, its oxidation product - malaoxon and isomerisation product - isomalathion inhibited AChE activity in a concentration-dependent manner. The half-maximum inhibitory concentrations (IC50 values): (3.2 +/- 0.1) x 10(-5) mol/l, (4.7 +/- 0.8) x 10(-7) mol/l and (6.0 +/- 0.5) x 10(-7) mol/l were obtained from the inhibition curves induced by malathion, malaoxon and isomalathion, respectively. However, the products formed due to photoinduced degradation, phosphorodithioic O,O,S-trimethyl phosphorodithioic ester (OOS(S)) and O,O-dimethyl thiophosphate did not noticeably affect the enzyme activity at all investigated concentrations, while diethyl maleate inhibited the AChE activity at concentrations GT 10 mmol/l. By simultaneous exposure of the enzyme to malaoxon and isomalathion in various concentration combinations the additive effect was achieved by low concentration of inhibitors, while the antagonistic effect was obtained at high concentration ( GT = 3 x 10-7 mol/l) of inhibitors. Inhibitory power of irradiated samples of 1 x 10(-5) mol/l malathion can be attributed to the formation of malaoxon and isomalathion, organophosphates about 100 times more toxic than their parent compound, while the presence of non-inhibiting degradation product OOS(S) did not affect the inhibitor efficiency of inhibiting malathion by-products, malaoxon and isomalathion.
T2  - General Physiology and Biophysics
T1  - Inhibition of AChE by single and simultaneous exposure to malathion and its degradation products
VL  - 26
IS  - 4
SP  - 247
EP  - 253
UR  - https://hdl.handle.net/21.15107/rcub_vinar_3364
ER  - 

@article{
author = "Krstić, Danijela Z. and Čolović, Mirjana B. and Krinulović, Katarina and Đurić, Dragan M. and Vasić, Vesna M.",
year = "2007",
abstract = "In vitro inhibition of bovine erythrocytes acetylcholinesterase (AchE) by separate and simultaneous exposure to organophosphorous insecticide malathion and the transformation products, which are generally formed during the storage or natural as well as photochemical degradation pathways of malathion, was investigated. The increasing concentration of malathion, its oxidation product - malaoxon and isomerisation product - isomalathion inhibited AChE activity in a concentration-dependent manner. The half-maximum inhibitory concentrations (IC50 values): (3.2 +/- 0.1) x 10(-5) mol/l, (4.7 +/- 0.8) x 10(-7) mol/l and (6.0 +/- 0.5) x 10(-7) mol/l were obtained from the inhibition curves induced by malathion, malaoxon and isomalathion, respectively. However, the products formed due to photoinduced degradation, phosphorodithioic O,O,S-trimethyl phosphorodithioic ester (OOS(S)) and O,O-dimethyl thiophosphate did not noticeably affect the enzyme activity at all investigated concentrations, while diethyl maleate inhibited the AChE activity at concentrations GT 10 mmol/l. By simultaneous exposure of the enzyme to malaoxon and isomalathion in various concentration combinations the additive effect was achieved by low concentration of inhibitors, while the antagonistic effect was obtained at high concentration ( GT = 3 x 10-7 mol/l) of inhibitors. Inhibitory power of irradiated samples of 1 x 10(-5) mol/l malathion can be attributed to the formation of malaoxon and isomalathion, organophosphates about 100 times more toxic than their parent compound, while the presence of non-inhibiting degradation product OOS(S) did not affect the inhibitor efficiency of inhibiting malathion by-products, malaoxon and isomalathion.",
journal = "General Physiology and Biophysics",
title = "Inhibition of AChE by single and simultaneous exposure to malathion and its degradation products",
volume = "26",
number = "4",
pages = "247-253",
url = "https://hdl.handle.net/21.15107/rcub_vinar_3364"
}

Krstić, D. Z., Čolović, M. B., Krinulović, K., Đurić, D. M.,& Vasić, V. M.. (2007). Inhibition of AChE by single and simultaneous exposure to malathion and its degradation products. in General Physiology and Biophysics, 26(4), 247-253.
https://hdl.handle.net/21.15107/rcub_vinar_3364

Krstić DZ, Čolović MB, Krinulović K, Đurić DM, Vasić VM. Inhibition of AChE by single and simultaneous exposure to malathion and its degradation products. in General Physiology and Biophysics. 2007;26(4):247-253.
https://hdl.handle.net/21.15107/rcub_vinar_3364 .

Krstić, Danijela Z., Čolović, Mirjana B., Krinulović, Katarina, Đurić, Dragan M., Vasić, Vesna M., "Inhibition of AChE by single and simultaneous exposure to malathion and its degradation products" in General Physiology and Biophysics, 26, no. 4 (2007):247-253,
https://hdl.handle.net/21.15107/rcub_vinar_3364 .

TY  - CONF
AU  - Krstić, Danijela Z.
AU  - Bavcon Kralj, Mojca
AU  - Trebše, Polonca
AU  - Čolović, Mirjana B.
AU  - Krinulović, Katarina
AU  - Vasić, Vesna M.
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9429
AB  - Inhibition of bovine serum acetylcholinesterase by in vitro exposure to malathion, malaoxon, isomalathion and diethyl maleate was investigated to elucidate the mechanism of the enzyme interaction with structurally similar organophosphorus compounds. IC50 (half maximum inhibitory concentrations) were determined by Hill analysis of experimentally obtained inhibition curves. The values (2.87 ± 0.24)x10-6 M, (2.65±0.61)x10-6M, (3.01±0.36)x10-4 M and (5.69 ±0.7)x10-2 M were obtained for malaoxon, isomalathion, malathion and their hydrolysis product diethyl maleate, respectively. The relationship between the structure of the compounds and their potency to inhibit the enzyme activity was discussed.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry
T1  - Inhibition of ache by malathion and some structuraly similar compounds
SP  - 401
EP  - 413
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9429
ER  - 

@conference{
author = "Krstić, Danijela Z. and Bavcon Kralj, Mojca and Trebše, Polonca and Čolović, Mirjana B. and Krinulović, Katarina and Vasić, Vesna M.",
year = "2006",
abstract = "Inhibition of bovine serum acetylcholinesterase by in vitro exposure to malathion, malaoxon, isomalathion and diethyl maleate was investigated to elucidate the mechanism of the enzyme interaction with structurally similar organophosphorus compounds. IC50 (half maximum inhibitory concentrations) were determined by Hill analysis of experimentally obtained inhibition curves. The values (2.87 ± 0.24)x10-6 M, (2.65±0.61)x10-6M, (3.01±0.36)x10-4 M and (5.69 ±0.7)x10-2 M were obtained for malaoxon, isomalathion, malathion and their hydrolysis product diethyl maleate, respectively. The relationship between the structure of the compounds and their potency to inhibit the enzyme activity was discussed.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry",
title = "Inhibition of ache by malathion and some structuraly similar compounds",
pages = "401-413",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9429"
}

Krstić, D. Z., Bavcon Kralj, M., Trebše, P., Čolović, M. B., Krinulović, K.,& Vasić, V. M.. (2006). Inhibition of ache by malathion and some structuraly similar compounds. in Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry
Society of Physical Chemists of Serbia., 401-413.
https://hdl.handle.net/21.15107/rcub_vinar_9429

Krstić DZ, Bavcon Kralj M, Trebše P, Čolović MB, Krinulović K, Vasić VM. Inhibition of ache by malathion and some structuraly similar compounds. in Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry. 2006;:401-413.
https://hdl.handle.net/21.15107/rcub_vinar_9429 .

Krstić, Danijela Z., Bavcon Kralj, Mojca, Trebše, Polonca, Čolović, Mirjana B., Krinulović, Katarina, Vasić, Vesna M., "Inhibition of ache by malathion and some structuraly similar compounds" in Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry (2006):401-413,
https://hdl.handle.net/21.15107/rcub_vinar_9429 .

TY  - JOUR
AU  - Krinulović, Katarina
AU  - Bugarčić, Živadin D.
AU  - Vrvić, Miroslav M.
AU  - Krstić, Danijela Z.
AU  - Vasić, Vesna M.
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3120
AB  - The effect of (mu(3)-diethylentriamino)-chloro-palladium(II)-chloride ([PdCl(dien)]Cl) on the activity of Na/K-ATPase from porcine cerebral cortex was studied in vitro, in the absence and presence of -SH containing ligandS L-cysteine and glutathione (GSH). The aim of the study was to elucidate the mechanism of [PdCl(dien)](+) induced inhibition of the enzyme activity and to examine the ability of thiols to prevent and recover the inhibition. The coordinative interaction between [PdCl(dien)](+) and enzyme was verified by UV and H-1 NMR spectra. The semblance in the changes in absorption spectra of [PdCl(dien)](+) in the presence of Na/K-ATPase and thiols (L-Cysteine and GSH) suggested that the complex ion interacts with enzymatic sulfhydryl groups. [PdCl(dien)](+) inhibited the enzyme activity in a dose-dependent manner. The Hill analysis of the inhibition curve yielded the half-maximum inhibitory activity value, IC50 = 1.21 x 10(-4) M, and Hill coefficient, n = 0.7, suggesting the negative cooperation for binding of [PdCl(dien)](+) to the enzyme. Dependence of the initial reaction rate on the concentration of MgATp(2-) exhibited typical Michelis-Menten kinetics in the absence and presence of the inhibitor. Kinetic analysis showed that [PdCl(dien)](+) inhibited Na/K-ATPase by reducing the maximum reaction rate (V-max), rather than changing the affinity to the substrate (Km). Kinetic parameters derived using Lineweaver-Burk transformation of experimental data indicated the non-competitive nature of Na/K-ATPase inhibition. The inhibitory constant, K-i = 1.05 x 10(-4) M, was determined from secondary replot of Lineweaver-Burk graph, and correlated with stability constants of [Pd(dien)(thiol)] complexes. 1 x 10(-3) M L-Cysteine or GSH prevented the enzyme inhibition induced by Pd(II) complex cation when present below 1 x 10(-4) M. The both thiols completely reversed the inhibited activity in the concentration dependent manner, due to the complex formation with [PdCl(dien)](+). (c) 2006 Elsevier Ltd. All rights reserved.
T2  - Toxicology in Vitro
T1  - Prevention and recovery of (mu(3)-diethylentriamino)-chloro-palladium(II)-chloride induced inhibition of Na/K-ATPase by SH containing ligands - L-cysteine and glutathione
VL  - 20
IS  - 8
SP  - 1292
EP  - 1299
DO  - 10.1016/j.tiv.2006.03.002
ER  - 

@article{
author = "Krinulović, Katarina and Bugarčić, Živadin D. and Vrvić, Miroslav M. and Krstić, Danijela Z. and Vasić, Vesna M.",
year = "2006",
abstract = "The effect of (mu(3)-diethylentriamino)-chloro-palladium(II)-chloride ([PdCl(dien)]Cl) on the activity of Na/K-ATPase from porcine cerebral cortex was studied in vitro, in the absence and presence of -SH containing ligandS L-cysteine and glutathione (GSH). The aim of the study was to elucidate the mechanism of [PdCl(dien)](+) induced inhibition of the enzyme activity and to examine the ability of thiols to prevent and recover the inhibition. The coordinative interaction between [PdCl(dien)](+) and enzyme was verified by UV and H-1 NMR spectra. The semblance in the changes in absorption spectra of [PdCl(dien)](+) in the presence of Na/K-ATPase and thiols (L-Cysteine and GSH) suggested that the complex ion interacts with enzymatic sulfhydryl groups. [PdCl(dien)](+) inhibited the enzyme activity in a dose-dependent manner. The Hill analysis of the inhibition curve yielded the half-maximum inhibitory activity value, IC50 = 1.21 x 10(-4) M, and Hill coefficient, n = 0.7, suggesting the negative cooperation for binding of [PdCl(dien)](+) to the enzyme. Dependence of the initial reaction rate on the concentration of MgATp(2-) exhibited typical Michelis-Menten kinetics in the absence and presence of the inhibitor. Kinetic analysis showed that [PdCl(dien)](+) inhibited Na/K-ATPase by reducing the maximum reaction rate (V-max), rather than changing the affinity to the substrate (Km). Kinetic parameters derived using Lineweaver-Burk transformation of experimental data indicated the non-competitive nature of Na/K-ATPase inhibition. The inhibitory constant, K-i = 1.05 x 10(-4) M, was determined from secondary replot of Lineweaver-Burk graph, and correlated with stability constants of [Pd(dien)(thiol)] complexes. 1 x 10(-3) M L-Cysteine or GSH prevented the enzyme inhibition induced by Pd(II) complex cation when present below 1 x 10(-4) M. The both thiols completely reversed the inhibited activity in the concentration dependent manner, due to the complex formation with [PdCl(dien)](+). (c) 2006 Elsevier Ltd. All rights reserved.",
journal = "Toxicology in Vitro",
title = "Prevention and recovery of (mu(3)-diethylentriamino)-chloro-palladium(II)-chloride induced inhibition of Na/K-ATPase by SH containing ligands - L-cysteine and glutathione",
volume = "20",
number = "8",
pages = "1292-1299",
doi = "10.1016/j.tiv.2006.03.002"
}

Krinulović, K., Bugarčić, Ž. D., Vrvić, M. M., Krstić, D. Z.,& Vasić, V. M.. (2006). Prevention and recovery of (mu(3)-diethylentriamino)-chloro-palladium(II)-chloride induced inhibition of Na/K-ATPase by SH containing ligands - L-cysteine and glutathione. in Toxicology in Vitro, 20(8), 1292-1299.
https://doi.org/10.1016/j.tiv.2006.03.002

Krinulović K, Bugarčić ŽD, Vrvić MM, Krstić DZ, Vasić VM. Prevention and recovery of (mu(3)-diethylentriamino)-chloro-palladium(II)-chloride induced inhibition of Na/K-ATPase by SH containing ligands - L-cysteine and glutathione. in Toxicology in Vitro. 2006;20(8):1292-1299.
doi:10.1016/j.tiv.2006.03.002 .

Krinulović, Katarina, Bugarčić, Živadin D., Vrvić, Miroslav M., Krstić, Danijela Z., Vasić, Vesna M., "Prevention and recovery of (mu(3)-diethylentriamino)-chloro-palladium(II)-chloride induced inhibition of Na/K-ATPase by SH containing ligands - L-cysteine and glutathione" in Toxicology in Vitro, 20, no. 8 (2006):1292-1299,
https://doi.org/10.1016/j.tiv.2006.03.002 . .

TY  - JOUR
AU  - Krstić, Danijela Z.
AU  - Tomić, Nenad
AU  - Krinulović, Katarina
AU  - Vasić, Vesna M.
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3081
AB  - The in vitro influence of potassium ion modulations, in the concentration range 2mM - 500mM, on digoxin-induced inhibition of porcine cerebral cortex Na+/K+-ATPase activity was studied. The response of enzymatic activity in the presence of various K+ concentrations to digoxin was biphasic, thereby, indicating the existence of two Na+/K+-ATPase isoforms, differing in the affinity towards the tested drug. Both isoforms showed higher sensitivity to digoxin in the presence of K+ ions below 20mM in the medium assay. The IC50 values for high/low isoforms 2.77 x 10(-6) M/8.56 x 10(-5) Mand 7.06 x 10(-7) M/1.87 x 10(-5) Mwere obtained in the presence of optimal (20mM) and 2mMK(+), respectively. However, preincubation in the presence of elevated K+ concentration (50 - 500mM) in the medium assay prior to Na+/K+-ATPase exposure to digoxin did not prevent the inhibition, i.e. IC50 values for both isoforms was the same as in the presence of the optimal K+ concentration. On the contrary, addition of 200mMK(+) into the medium assay after 10 minutes exposure of Na+/K+-ATPase to digoxin, showed a time-dependent recovery effect on the inhibited enzymatic activity. Kinetic analysis showed that digoxin inhibited Na+/K+-ATPase by reducing maximum enzymatic velocity (V-max) and K-m, implying an uncompetitive mode of interaction.
T2  - Journal of Enzyme Inhibition and Medicinal Chemistry
T1  - The influence of potassium ion (K+) on digoxin-induced inhibition of porcine cerebral cortex Na+/K+-ATPase
VL  - 21
IS  - 4
SP  - 471
EP  - 475
DO  - 10.1080/14756360600642230
ER  - 

@article{
author = "Krstić, Danijela Z. and Tomić, Nenad and Krinulović, Katarina and Vasić, Vesna M.",
year = "2006",
abstract = "The in vitro influence of potassium ion modulations, in the concentration range 2mM - 500mM, on digoxin-induced inhibition of porcine cerebral cortex Na+/K+-ATPase activity was studied. The response of enzymatic activity in the presence of various K+ concentrations to digoxin was biphasic, thereby, indicating the existence of two Na+/K+-ATPase isoforms, differing in the affinity towards the tested drug. Both isoforms showed higher sensitivity to digoxin in the presence of K+ ions below 20mM in the medium assay. The IC50 values for high/low isoforms 2.77 x 10(-6) M/8.56 x 10(-5) Mand 7.06 x 10(-7) M/1.87 x 10(-5) Mwere obtained in the presence of optimal (20mM) and 2mMK(+), respectively. However, preincubation in the presence of elevated K+ concentration (50 - 500mM) in the medium assay prior to Na+/K+-ATPase exposure to digoxin did not prevent the inhibition, i.e. IC50 values for both isoforms was the same as in the presence of the optimal K+ concentration. On the contrary, addition of 200mMK(+) into the medium assay after 10 minutes exposure of Na+/K+-ATPase to digoxin, showed a time-dependent recovery effect on the inhibited enzymatic activity. Kinetic analysis showed that digoxin inhibited Na+/K+-ATPase by reducing maximum enzymatic velocity (V-max) and K-m, implying an uncompetitive mode of interaction.",
journal = "Journal of Enzyme Inhibition and Medicinal Chemistry",
title = "The influence of potassium ion (K+) on digoxin-induced inhibition of porcine cerebral cortex Na+/K+-ATPase",
volume = "21",
number = "4",
pages = "471-475",
doi = "10.1080/14756360600642230"
}

Krstić, D. Z., Tomić, N., Krinulović, K.,& Vasić, V. M.. (2006). The influence of potassium ion (K+) on digoxin-induced inhibition of porcine cerebral cortex Na+/K+-ATPase. in Journal of Enzyme Inhibition and Medicinal Chemistry, 21(4), 471-475.
https://doi.org/10.1080/14756360600642230

Krstić DZ, Tomić N, Krinulović K, Vasić VM. The influence of potassium ion (K+) on digoxin-induced inhibition of porcine cerebral cortex Na+/K+-ATPase. in Journal of Enzyme Inhibition and Medicinal Chemistry. 2006;21(4):471-475.
doi:10.1080/14756360600642230 .

Krstić, Danijela Z., Tomić, Nenad, Krinulović, Katarina, Vasić, Vesna M., "The influence of potassium ion (K+) on digoxin-induced inhibition of porcine cerebral cortex Na+/K+-ATPase" in Journal of Enzyme Inhibition and Medicinal Chemistry, 21, no. 4 (2006):471-475,
https://doi.org/10.1080/14756360600642230 . .

TY  - JOUR
AU  - Krinulović, Katarina
AU  - Vasić, Vesna M.
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3080
AB  - The aim of this work was to investigate the influence of [PdCl4](2-), [PdCl(dien)](+) and [PdCl(Me(4)dien)](+) complexes on Na+/K+-ATPase activity. The dose-dependent inhibition curves were obtained in all cases. IC50 values determined by Hill analysis were 2.25 x 10(-5) M, 1.21 x 10(-4) Mand 2.36 x 10(-4) M, respectively. Na+/K+-ATPase exhibited typical Michelis-Menten kinetics in the presence of Pd(II) complexes. Kinetic parameters (V-max, K-m) derived using Eadie - Hofstee transformation indicated a noncompetitive type of Na+/K+-ATPase inhibition. The inhibitor constants (K-i) were determined from Dixon plots. The order of complex affinity for binding with Na+/K+-ATPase, deducted from K-i values, was [PdCl4](2-) GT [PdCl(dien)]+ GT [ PdCl(Me(4)dien)](+). The results indicated that the potency of Pd(II) complexes to inhibit Na+/K+-ATPase activity depended strongly on ligands of the related compound. Furthermore, the ability of SH-donor ligands, L-cysteine and glutathione, to prevent and recover the Pd(II) complexes-induced inhibition of Na+/K+-ATPase was examined. The addition of 1mM L-cysteine or glutathione to the reaction mixture before exposure to Pd(II) complexes prevented the inhibition by increasing the IC50 values by one order of magnitude. Moreover, the inhibited enzymatic activity was recovered by addition of SH-donor ligands in a concentration-dependent manner.
T2  - Journal of Enzyme Inhibition and Medicinal Chemistry
T1  - Interaction of some pd(II) complexes with Na+/K+-ATPase: Inhibition, kinetics, prevention and recovery
VL  - 21
IS  - 4
SP  - 459
EP  - 465
DO  - 10.1080/14756360600628510
ER  - 

@article{
author = "Krinulović, Katarina and Vasić, Vesna M.",
year = "2006",
abstract = "The aim of this work was to investigate the influence of [PdCl4](2-), [PdCl(dien)](+) and [PdCl(Me(4)dien)](+) complexes on Na+/K+-ATPase activity. The dose-dependent inhibition curves were obtained in all cases. IC50 values determined by Hill analysis were 2.25 x 10(-5) M, 1.21 x 10(-4) Mand 2.36 x 10(-4) M, respectively. Na+/K+-ATPase exhibited typical Michelis-Menten kinetics in the presence of Pd(II) complexes. Kinetic parameters (V-max, K-m) derived using Eadie - Hofstee transformation indicated a noncompetitive type of Na+/K+-ATPase inhibition. The inhibitor constants (K-i) were determined from Dixon plots. The order of complex affinity for binding with Na+/K+-ATPase, deducted from K-i values, was [PdCl4](2-) GT [PdCl(dien)]+ GT [ PdCl(Me(4)dien)](+). The results indicated that the potency of Pd(II) complexes to inhibit Na+/K+-ATPase activity depended strongly on ligands of the related compound. Furthermore, the ability of SH-donor ligands, L-cysteine and glutathione, to prevent and recover the Pd(II) complexes-induced inhibition of Na+/K+-ATPase was examined. The addition of 1mM L-cysteine or glutathione to the reaction mixture before exposure to Pd(II) complexes prevented the inhibition by increasing the IC50 values by one order of magnitude. Moreover, the inhibited enzymatic activity was recovered by addition of SH-donor ligands in a concentration-dependent manner.",
journal = "Journal of Enzyme Inhibition and Medicinal Chemistry",
title = "Interaction of some pd(II) complexes with Na+/K+-ATPase: Inhibition, kinetics, prevention and recovery",
volume = "21",
number = "4",
pages = "459-465",
doi = "10.1080/14756360600628510"
}

Krinulović, K.,& Vasić, V. M.. (2006). Interaction of some pd(II) complexes with Na+/K+-ATPase: Inhibition, kinetics, prevention and recovery. in Journal of Enzyme Inhibition and Medicinal Chemistry, 21(4), 459-465.
https://doi.org/10.1080/14756360600628510

Krinulović K, Vasić VM. Interaction of some pd(II) complexes with Na+/K+-ATPase: Inhibition, kinetics, prevention and recovery. in Journal of Enzyme Inhibition and Medicinal Chemistry. 2006;21(4):459-465.
doi:10.1080/14756360600628510 .

Krinulović, Katarina, Vasić, Vesna M., "Interaction of some pd(II) complexes with Na+/K+-ATPase: Inhibition, kinetics, prevention and recovery" in Journal of Enzyme Inhibition and Medicinal Chemistry, 21, no. 4 (2006):459-465,
https://doi.org/10.1080/14756360600628510 . .

TY  - JOUR
AU  - Vasić, Vesna M.
AU  - Černigoj, Urh
AU  - Krinulović, Katarina
AU  - Joksić, Gordana
AU  - Franko, Mladen
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2972
AB  - A simple Na,K-ATPase assay is described as a suitable method for testing of digoxin photodegradation. The exposure of Na,K-ATPase to the photodegraded samples exhibited reduced inhibition of the enzyme, compared to the unirradiated samples containing equal initial concentrations of drug. The degree of inhibition was dependent on the irradiation time. The concentrations of digoxin in irradiated samples were evaluated by HPLC analysis. Excellent agreement of the results obtained by both methods was observed. The investigation of the influence of irradiated samples on Na,K-ATPase inhibition revealed no side products acting as Na,K-ATPase inhibitors. The cytokinesis block micronucleus test (CBMN) was applied in order to investigate the cytotoxicity of the possible degradation products after exposure to UV irradiation. The results confirmed that the photochemical treatment did not induce the cytotoxic side products. Zero order kinetics, which was observed for digoxin photodegradation and the associated reaction mechanism are also discussed. (c) 2005 Elsevier B.V. All rights reserved.
T2  - Journal of Pharmaceutical and Biomedical Analysis
T1  - Evaluation of photochemical degradation of digoxin by Na,K-ATPase assay
VL  - 40
IS  - 2
SP  - 404
EP  - 409
DO  - 10.1016/j.jpba.2005.05.018
ER  - 

@article{
author = "Vasić, Vesna M. and Černigoj, Urh and Krinulović, Katarina and Joksić, Gordana and Franko, Mladen",
year = "2006",
abstract = "A simple Na,K-ATPase assay is described as a suitable method for testing of digoxin photodegradation. The exposure of Na,K-ATPase to the photodegraded samples exhibited reduced inhibition of the enzyme, compared to the unirradiated samples containing equal initial concentrations of drug. The degree of inhibition was dependent on the irradiation time. The concentrations of digoxin in irradiated samples were evaluated by HPLC analysis. Excellent agreement of the results obtained by both methods was observed. The investigation of the influence of irradiated samples on Na,K-ATPase inhibition revealed no side products acting as Na,K-ATPase inhibitors. The cytokinesis block micronucleus test (CBMN) was applied in order to investigate the cytotoxicity of the possible degradation products after exposure to UV irradiation. The results confirmed that the photochemical treatment did not induce the cytotoxic side products. Zero order kinetics, which was observed for digoxin photodegradation and the associated reaction mechanism are also discussed. (c) 2005 Elsevier B.V. All rights reserved.",
journal = "Journal of Pharmaceutical and Biomedical Analysis",
title = "Evaluation of photochemical degradation of digoxin by Na,K-ATPase assay",
volume = "40",
number = "2",
pages = "404-409",
doi = "10.1016/j.jpba.2005.05.018"
}

Vasić, V. M., Černigoj, U., Krinulović, K., Joksić, G.,& Franko, M.. (2006). Evaluation of photochemical degradation of digoxin by Na,K-ATPase assay. in Journal of Pharmaceutical and Biomedical Analysis, 40(2), 404-409.
https://doi.org/10.1016/j.jpba.2005.05.018

Vasić VM, Černigoj U, Krinulović K, Joksić G, Franko M. Evaluation of photochemical degradation of digoxin by Na,K-ATPase assay. in Journal of Pharmaceutical and Biomedical Analysis. 2006;40(2):404-409.
doi:10.1016/j.jpba.2005.05.018 .

Vasić, Vesna M., Černigoj, Urh, Krinulović, Katarina, Joksić, Gordana, Franko, Mladen, "Evaluation of photochemical degradation of digoxin by Na,K-ATPase assay" in Journal of Pharmaceutical and Biomedical Analysis, 40, no. 2 (2006):404-409,
https://doi.org/10.1016/j.jpba.2005.05.018 . .

TY  - CONF
AU  - Krinulović, Katarina
AU  - Vasić, Vesna M.
AU  - Krstić, Danijela Z.
PY  - 2005
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/6585
AB  - The possibility of using enzyme Na+/K+-ATPase as a biological component of sensing system for detection of toxic metal ions (Hg2+, Pb2+ and Cd2+) in water samples has been studied. The method is based on the spectrophotometric determination of inorganic orthophosphate (P) that serves as a measure of the enzymatic activity in the presence of considered metal ions. The concentration of Pi, liberated by enzyme catalysed hydrolysis of adenosinetriphosphate (ATP), was followed spectrophotometrically, by single exposure to analytes or in the mixture. Hg2+, Pb2+ and Cd2+ induced the dose-dependent inhibition of Na+/K+-ATPase activity in enzymatic mixture. Sigmoid shaped inhibition curves were obtained in all cases. Half-maximum inhibitory activities (IC50) were determined by fitting the experimental data by sigmoid function. Considering Na+/K+-ATPase high sensibility to toxic metal ions, the development of simple and quick method for preliminary detection of water contamination by metals based on enzymatic activity measurement was suggested.
T1  - Detection of toxic metal ions in water based on Na+/K+-ATPase activity measurement
SP  - B479
EP  - B484
UR  - https://hdl.handle.net/21.15107/rcub_vinar_6585
ER  - 

@conference{
author = "Krinulović, Katarina and Vasić, Vesna M. and Krstić, Danijela Z.",
year = "2005",
abstract = "The possibility of using enzyme Na+/K+-ATPase as a biological component of sensing system for detection of toxic metal ions (Hg2+, Pb2+ and Cd2+) in water samples has been studied. The method is based on the spectrophotometric determination of inorganic orthophosphate (P) that serves as a measure of the enzymatic activity in the presence of considered metal ions. The concentration of Pi, liberated by enzyme catalysed hydrolysis of adenosinetriphosphate (ATP), was followed spectrophotometrically, by single exposure to analytes or in the mixture. Hg2+, Pb2+ and Cd2+ induced the dose-dependent inhibition of Na+/K+-ATPase activity in enzymatic mixture. Sigmoid shaped inhibition curves were obtained in all cases. Half-maximum inhibitory activities (IC50) were determined by fitting the experimental data by sigmoid function. Considering Na+/K+-ATPase high sensibility to toxic metal ions, the development of simple and quick method for preliminary detection of water contamination by metals based on enzymatic activity measurement was suggested.",
title = "Detection of toxic metal ions in water based on Na+/K+-ATPase activity measurement",
pages = "B479-B484",
url = "https://hdl.handle.net/21.15107/rcub_vinar_6585"
}

Krinulović, K., Vasić, V. M.,& Krstić, D. Z.. (2005). Detection of toxic metal ions in water based on Na+/K+-ATPase activity measurement. , B479-B484.
https://hdl.handle.net/21.15107/rcub_vinar_6585

Krinulović K, Vasić VM, Krstić DZ. Detection of toxic metal ions in water based on Na+/K+-ATPase activity measurement. 2005;:B479-B484.
https://hdl.handle.net/21.15107/rcub_vinar_6585 .

Krinulović, Katarina, Vasić, Vesna M., Krstić, Danijela Z., "Detection of toxic metal ions in water based on Na+/K+-ATPase activity measurement" (2005):B479-B484,
https://hdl.handle.net/21.15107/rcub_vinar_6585 .

TY  - JOUR
AU  - Krstić, Danijela Z.
AU  - Krinulović, Katarina
AU  - Vasić, Vesna M.
PY  - 2005
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2947
AB  - Kinetics and inhibition of Na+/K+-ATPase and Mg2+-ATPase activity from rat synaptic plasma membrane (SPM), by separate and simultaneous exposure to transition (Cu2+, Zn2+, Fe2+ and Co2+) and heavy metals (Hg(2+)and Pb2+) ions were studied. All investigated metals produced a larger maximum inhibition of Na+/K+-ATPase than Mg2+-ATPase activity. The free concentrations of the key species (inhibitor, MgATp(2-), MeATp(2-)) in the medium assay were calculated and discussed. Simultaneous exposure to the combinations Cu2+/Fe2+ or Hg2+/Pb(2+)caused additive inhibition, while Cu2+/Zn2+ or Fe2+/Zn2+ inhibited Na+/K+-ATPase activity synergistically (i.e., greater than the sum metal-induced inhibition assayed separately). Simultaneous exposure to Cu2+/Fe2+ or Cu2+/Zn2+ inhibited Mg2+-ATPase activity synergistically, while Hg2+/Pb2+ or Fe2+/Zn2+ induced antagonistic inhibition of this enzyme. Kinetic analysis showed that all investigated metals inhibited Na+/K+-ATPase activity by reducing the maximum velocities (V-max) rather than the apparent affinity (K-m) for substrate MgATp(2-), implying the noncompetitive nature of the inhibition. The incomplete inhibition of Mg2+-ATPase activity by Zn2+, Fe2+ and Co2+ as well as kinetic analysis indicated two distinct Mg2+-ATPase subtypes activated in the presence of low and high MgATp2- concentration. EDTA, L-cysteine and gluthathione (GSH) prevented metal ion-induced inhibition of Na+/K+-ATPase with various potencies. Furthermore, these ligands also reversed Na+/K+-ATPase activity inhibited by transition metals in a concentration-dependent manner, but a recovery effect by any ligand on Hg2+-induced inhibition was not obtained.
T2  - Journal of Enzyme Inhibition and Medicinal Chemistry
T1  - Inhibition of Na+/K+-ATPase and Mg2+-ATPase by metal ions and prevention and recovery of inhibited activities by chelators
VL  - 20
IS  - 5
SP  - 469
EP  - 476
DO  - 10.1080/14756360500213280
ER  - 

@article{
author = "Krstić, Danijela Z. and Krinulović, Katarina and Vasić, Vesna M.",
year = "2005",
abstract = "Kinetics and inhibition of Na+/K+-ATPase and Mg2+-ATPase activity from rat synaptic plasma membrane (SPM), by separate and simultaneous exposure to transition (Cu2+, Zn2+, Fe2+ and Co2+) and heavy metals (Hg(2+)and Pb2+) ions were studied. All investigated metals produced a larger maximum inhibition of Na+/K+-ATPase than Mg2+-ATPase activity. The free concentrations of the key species (inhibitor, MgATp(2-), MeATp(2-)) in the medium assay were calculated and discussed. Simultaneous exposure to the combinations Cu2+/Fe2+ or Hg2+/Pb(2+)caused additive inhibition, while Cu2+/Zn2+ or Fe2+/Zn2+ inhibited Na+/K+-ATPase activity synergistically (i.e., greater than the sum metal-induced inhibition assayed separately). Simultaneous exposure to Cu2+/Fe2+ or Cu2+/Zn2+ inhibited Mg2+-ATPase activity synergistically, while Hg2+/Pb2+ or Fe2+/Zn2+ induced antagonistic inhibition of this enzyme. Kinetic analysis showed that all investigated metals inhibited Na+/K+-ATPase activity by reducing the maximum velocities (V-max) rather than the apparent affinity (K-m) for substrate MgATp(2-), implying the noncompetitive nature of the inhibition. The incomplete inhibition of Mg2+-ATPase activity by Zn2+, Fe2+ and Co2+ as well as kinetic analysis indicated two distinct Mg2+-ATPase subtypes activated in the presence of low and high MgATp2- concentration. EDTA, L-cysteine and gluthathione (GSH) prevented metal ion-induced inhibition of Na+/K+-ATPase with various potencies. Furthermore, these ligands also reversed Na+/K+-ATPase activity inhibited by transition metals in a concentration-dependent manner, but a recovery effect by any ligand on Hg2+-induced inhibition was not obtained.",
journal = "Journal of Enzyme Inhibition and Medicinal Chemistry",
title = "Inhibition of Na+/K+-ATPase and Mg2+-ATPase by metal ions and prevention and recovery of inhibited activities by chelators",
volume = "20",
number = "5",
pages = "469-476",
doi = "10.1080/14756360500213280"
}

Krstić, D. Z., Krinulović, K.,& Vasić, V. M.. (2005). Inhibition of Na+/K+-ATPase and Mg2+-ATPase by metal ions and prevention and recovery of inhibited activities by chelators. in Journal of Enzyme Inhibition and Medicinal Chemistry, 20(5), 469-476.
https://doi.org/10.1080/14756360500213280

Krstić DZ, Krinulović K, Vasić VM. Inhibition of Na+/K+-ATPase and Mg2+-ATPase by metal ions and prevention and recovery of inhibited activities by chelators. in Journal of Enzyme Inhibition and Medicinal Chemistry. 2005;20(5):469-476.
doi:10.1080/14756360500213280 .

Krstić, Danijela Z., Krinulović, Katarina, Vasić, Vesna M., "Inhibition of Na+/K+-ATPase and Mg2+-ATPase by metal ions and prevention and recovery of inhibited activities by chelators" in Journal of Enzyme Inhibition and Medicinal Chemistry, 20, no. 5 (2005):469-476,
https://doi.org/10.1080/14756360500213280 . .

TY  - CONF
AU  - Krinulović, Katarina
AU  - Vasić, Vesna M.
AU  - Černigoj, Urh
AU  - Franko, Mladen
PY  - 2004
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9584
AB  - The photochemical degradation of digoxin aqueous solution was obtained by Xelamp irradiation. The concentrations of digoxin in irradiated solutions were detected by measurements of Na,K-ATPase activity and by HPLC analysis. The excellent agreement using two independent methods for determination of digoxin concentration in the irradiated samples was achieved.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry
T1  - Photochemical degradation of digoxin tested by Na,K-ATPase activity
VL  - 2
SP  - 694
EP  - 696
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9584
ER  - 

@conference{
author = "Krinulović, Katarina and Vasić, Vesna M. and Černigoj, Urh and Franko, Mladen",
year = "2004",
abstract = "The photochemical degradation of digoxin aqueous solution was obtained by Xelamp irradiation. The concentrations of digoxin in irradiated solutions were detected by measurements of Na,K-ATPase activity and by HPLC analysis. The excellent agreement using two independent methods for determination of digoxin concentration in the irradiated samples was achieved.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry",
title = "Photochemical degradation of digoxin tested by Na,K-ATPase activity",
volume = "2",
pages = "694-696",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9584"
}

Krinulović, K., Vasić, V. M., Černigoj, U.,& Franko, M.. (2004). Photochemical degradation of digoxin tested by Na,K-ATPase activity. in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry
Society of Physical Chemists of Serbia., 2, 694-696.
https://hdl.handle.net/21.15107/rcub_vinar_9584

Krinulović K, Vasić VM, Černigoj U, Franko M. Photochemical degradation of digoxin tested by Na,K-ATPase activity. in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry. 2004;2:694-696.
https://hdl.handle.net/21.15107/rcub_vinar_9584 .

Krinulović, Katarina, Vasić, Vesna M., Černigoj, Urh, Franko, Mladen, "Photochemical degradation of digoxin tested by Na,K-ATPase activity" in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry, 2 (2004):694-696,
https://hdl.handle.net/21.15107/rcub_vinar_9584 .

TY  - JOUR
AU  - Krstić, Danijela Z.
AU  - Krinulović, Katarina
AU  - Spasojević-Tišma, Vera D.
AU  - Joksić, Gordana
AU  - Momić, Tatjana
AU  - Vasić, Vesna M.
PY  - 2004
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2838
AB  - Inhibition of Na+/K+-ATPase activity from human erythrocyte membranes and commercial porcine cerebral cortex by in vitro single and simultaneous exposure to digoxin and gitoxin was investigated to elucidate the difference in the mechanism of the enzyme inhibition by structurally different cardiac glycosides. The drugs exerted a biphasic dose-dependent inhibitory effect on the enzyme activity in both tissues, supporting the existence of two sensitive Na+/K+-ATPase isoforms. The IC50 values for the low and high affinity isoforms were calculated from the inhibition curves using mathematical analysis. The Hill coefficient (n) fulfilled the relationship 1 LT n LT 3; suggesting cooperative binding of inhibitors to the enzyme. Kinetic analysis showed that digoxin and gitoxin inhibited Na+/K+-ATPase by reducing the maximum enzymatic velocity (V-max) and K-m, implying an uncompetitive mode of interaction. Both the isoforms were always more sensitive to gitoxin. The erythrocyte enzyme was more sensitive to the inhibitors in the range of low concentrations but the commercial cerebral cortex enzyme exerted a higher sensitivity in high inhibitors affinity concentration range. By simultaneous exposure of the enzyme to digoxin and gitoxin in combinations a synergistic effect was achieved by low inhibitor concentrations. An antagonistic effect was obtained with erythrocyte membrane enzyme at high inhibitors concentration.
T2  - Journal of Enzyme Inhibition and Medicinal Chemistry
T1  - Effects of digoxin and gitoxin on the enzymatic activity and kinetic parameters of Na+/K+-ATPase
VL  - 19
IS  - 5
SP  - 409
EP  - 415
DO  - 10.1080/14756360410001722065
ER  - 

@article{
author = "Krstić, Danijela Z. and Krinulović, Katarina and Spasojević-Tišma, Vera D. and Joksić, Gordana and Momić, Tatjana and Vasić, Vesna M.",
year = "2004",
abstract = "Inhibition of Na+/K+-ATPase activity from human erythrocyte membranes and commercial porcine cerebral cortex by in vitro single and simultaneous exposure to digoxin and gitoxin was investigated to elucidate the difference in the mechanism of the enzyme inhibition by structurally different cardiac glycosides. The drugs exerted a biphasic dose-dependent inhibitory effect on the enzyme activity in both tissues, supporting the existence of two sensitive Na+/K+-ATPase isoforms. The IC50 values for the low and high affinity isoforms were calculated from the inhibition curves using mathematical analysis. The Hill coefficient (n) fulfilled the relationship 1 LT n LT 3; suggesting cooperative binding of inhibitors to the enzyme. Kinetic analysis showed that digoxin and gitoxin inhibited Na+/K+-ATPase by reducing the maximum enzymatic velocity (V-max) and K-m, implying an uncompetitive mode of interaction. Both the isoforms were always more sensitive to gitoxin. The erythrocyte enzyme was more sensitive to the inhibitors in the range of low concentrations but the commercial cerebral cortex enzyme exerted a higher sensitivity in high inhibitors affinity concentration range. By simultaneous exposure of the enzyme to digoxin and gitoxin in combinations a synergistic effect was achieved by low inhibitor concentrations. An antagonistic effect was obtained with erythrocyte membrane enzyme at high inhibitors concentration.",
journal = "Journal of Enzyme Inhibition and Medicinal Chemistry",
title = "Effects of digoxin and gitoxin on the enzymatic activity and kinetic parameters of Na+/K+-ATPase",
volume = "19",
number = "5",
pages = "409-415",
doi = "10.1080/14756360410001722065"
}

Krstić, D. Z., Krinulović, K., Spasojević-Tišma, V. D., Joksić, G., Momić, T.,& Vasić, V. M.. (2004). Effects of digoxin and gitoxin on the enzymatic activity and kinetic parameters of Na+/K+-ATPase. in Journal of Enzyme Inhibition and Medicinal Chemistry, 19(5), 409-415.
https://doi.org/10.1080/14756360410001722065

Krstić DZ, Krinulović K, Spasojević-Tišma VD, Joksić G, Momić T, Vasić VM. Effects of digoxin and gitoxin on the enzymatic activity and kinetic parameters of Na+/K+-ATPase. in Journal of Enzyme Inhibition and Medicinal Chemistry. 2004;19(5):409-415.
doi:10.1080/14756360410001722065 .

Krstić, Danijela Z., Krinulović, Katarina, Spasojević-Tišma, Vera D., Joksić, Gordana, Momić, Tatjana, Vasić, Vesna M., "Effects of digoxin and gitoxin on the enzymatic activity and kinetic parameters of Na+/K+-ATPase" in Journal of Enzyme Inhibition and Medicinal Chemistry, 19, no. 5 (2004):409-415,
https://doi.org/10.1080/14756360410001722065 . .

TY  - JOUR
AU  - Vujisić Lj.
AU  - Krstić, Danijela Z.
AU  - Krinulović, Katarina
AU  - Vasić, Vesna M.
PY  - 2004
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2789
AB  - The influence of transition metal (Cu2-,Zn2+, Fe2+ and Co2+) and heavy metal ions (Hg2+, Ph2+ and Cd2+) on the activities of Na+/K+-ATPase and Mg2+-ATPase isolated from rat synaptic plasma membranes (SPM) was investigated. The aim of the study was to elucidate the inhibition of both ATPase activities by exposure to the considered metal ions as a function of their affinity to bind to the -SH containing ligand L-cysteine, as a model system. The half-maximum inhibitory activities (IC50) of the enzymes were determined as parameters of rectangular hyperbolas and correlated with the stability constant (K-s) of the respective metal-ion-L-cysteine complex. The linear Dixon plots indicate equilibrium binding of the investigated ions to both enzymes.
T2  - Journal of the Serbian Chemical Society
T1  - The influence of transition and heavy metal ions on ATP-ases activity in rat synaptic plasma membranes
VL  - 69
IS  - 7
SP  - 541
EP  - 547
DO  - 10.2298/JSC0407541V
ER  - 

@article{
author = "Vujisić Lj. and Krstić, Danijela Z. and Krinulović, Katarina and Vasić, Vesna M.",
year = "2004",
abstract = "The influence of transition metal (Cu2-,Zn2+, Fe2+ and Co2+) and heavy metal ions (Hg2+, Ph2+ and Cd2+) on the activities of Na+/K+-ATPase and Mg2+-ATPase isolated from rat synaptic plasma membranes (SPM) was investigated. The aim of the study was to elucidate the inhibition of both ATPase activities by exposure to the considered metal ions as a function of their affinity to bind to the -SH containing ligand L-cysteine, as a model system. The half-maximum inhibitory activities (IC50) of the enzymes were determined as parameters of rectangular hyperbolas and correlated with the stability constant (K-s) of the respective metal-ion-L-cysteine complex. The linear Dixon plots indicate equilibrium binding of the investigated ions to both enzymes.",
journal = "Journal of the Serbian Chemical Society",
title = "The influence of transition and heavy metal ions on ATP-ases activity in rat synaptic plasma membranes",
volume = "69",
number = "7",
pages = "541-547",
doi = "10.2298/JSC0407541V"
}

Vujisić Lj., Krstić, D. Z., Krinulović, K.,& Vasić, V. M.. (2004). The influence of transition and heavy metal ions on ATP-ases activity in rat synaptic plasma membranes. in Journal of the Serbian Chemical Society, 69(7), 541-547.
https://doi.org/10.2298/JSC0407541V

Vujisić Lj., Krstić DZ, Krinulović K, Vasić VM. The influence of transition and heavy metal ions on ATP-ases activity in rat synaptic plasma membranes. in Journal of the Serbian Chemical Society. 2004;69(7):541-547.
doi:10.2298/JSC0407541V .

Vujisić Lj., Krstić, Danijela Z., Krinulović, Katarina, Vasić, Vesna M., "The influence of transition and heavy metal ions on ATP-ases activity in rat synaptic plasma membranes" in Journal of the Serbian Chemical Society, 69, no. 7 (2004):541-547,
https://doi.org/10.2298/JSC0407541V . .

TY  - JOUR
AU  - Vasić, Vesna M.
AU  - Krinulović, Katarina
AU  - Krstić, Danijela Z.
AU  - Momić, Tatjana
AU  - Horvat, Anica
PY  - 2004
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2765
AB  - The possibility of using synaptic plasma membrane (SPM) enzymes Na+/K+-ATPase and Mg2+-ATPase, isolated from rat brain, as a biological component of multi-response sensing system for detection of different compounds (alkaline and heavy metal salts, organic compounds) was studied. The method is based on the spectrophotometric determination of inorganic ortho-phosphate (P-i) that serves as a measure of the enzymatic activity in the presence of various analytes. The concentration of P-i, liberated by enzyme catalysed hydrolysis of adenosinetriphosphate (ATP), was followed spectrophotometrically, by single exposure to analytes or in the mixture. P-i was dose dependent on the analyte concentration. Alkaline elements (Na, K, Mg), heavy metals (Pb, Cd, Hg, Cu, Fe, Co, Zn), toxic organic compounds (pyridine, urea, chlorpyrifos), and some drugs (digoxin, gitoxin) showed diverse effects, inducing the inhibition or stimulation of the enzymes activity. Development of simple test method for simultaneous detection of the investigated analytes based on the variation of medium assay composition was discussed.
T2  - Monatshefte Fur Chemie
T1  - ATPases as multi-response sensing system for various organic and inorganic analytes
VL  - 135
IS  - 5
SP  - 605
EP  - 614
DO  - 10.1007/s00706-003-0156-4
ER  - 

@article{
author = "Vasić, Vesna M. and Krinulović, Katarina and Krstić, Danijela Z. and Momić, Tatjana and Horvat, Anica",
year = "2004",
abstract = "The possibility of using synaptic plasma membrane (SPM) enzymes Na+/K+-ATPase and Mg2+-ATPase, isolated from rat brain, as a biological component of multi-response sensing system for detection of different compounds (alkaline and heavy metal salts, organic compounds) was studied. The method is based on the spectrophotometric determination of inorganic ortho-phosphate (P-i) that serves as a measure of the enzymatic activity in the presence of various analytes. The concentration of P-i, liberated by enzyme catalysed hydrolysis of adenosinetriphosphate (ATP), was followed spectrophotometrically, by single exposure to analytes or in the mixture. P-i was dose dependent on the analyte concentration. Alkaline elements (Na, K, Mg), heavy metals (Pb, Cd, Hg, Cu, Fe, Co, Zn), toxic organic compounds (pyridine, urea, chlorpyrifos), and some drugs (digoxin, gitoxin) showed diverse effects, inducing the inhibition or stimulation of the enzymes activity. Development of simple test method for simultaneous detection of the investigated analytes based on the variation of medium assay composition was discussed.",
journal = "Monatshefte Fur Chemie",
title = "ATPases as multi-response sensing system for various organic and inorganic analytes",
volume = "135",
number = "5",
pages = "605-614",
doi = "10.1007/s00706-003-0156-4"
}

Vasić, V. M., Krinulović, K., Krstić, D. Z., Momić, T.,& Horvat, A.. (2004). ATPases as multi-response sensing system for various organic and inorganic analytes. in Monatshefte Fur Chemie, 135(5), 605-614.
https://doi.org/10.1007/s00706-003-0156-4

Vasić VM, Krinulović K, Krstić DZ, Momić T, Horvat A. ATPases as multi-response sensing system for various organic and inorganic analytes. in Monatshefte Fur Chemie. 2004;135(5):605-614.
doi:10.1007/s00706-003-0156-4 .

Vasić, Vesna M., Krinulović, Katarina, Krstić, Danijela Z., Momić, Tatjana, Horvat, Anica, "ATPases as multi-response sensing system for various organic and inorganic analytes" in Monatshefte Fur Chemie, 135, no. 5 (2004):605-614,
https://doi.org/10.1007/s00706-003-0156-4 . .

TY  - CONF
AU  - Krinulović, Katarina
PY  - 2004
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9489
AB  - The effects of some Pd(II) complexes on Na,K-ATPase were studied by kinetic analysis. Na,K-ATPase obeyed Michaelis-Menten kinetics in the absence and presence of [PdCl4] 2-, [Pd(dien)Cl]+  and [Pd(Me4dien)Cl]+ . The kinetic parameters (Km and Vmax) showed that Pd(II) complexes are noncompetitive inhibitors of Na,K-ATPase. Based on the values of inhibitor constants (Ki) determined from Dixon plots, we concluded that Pd(II) complex potency to inhibit the Na,K-ATPase activity depends on steric bulkness of its ligands.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry
T1  - The mechanism of interference of some Pd(II) complexes with Na,K-ATPase activity - kinetic analysis
VL  - 1
SP  - 237
EP  - 239
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9489
ER  - 

@conference{
author = "Krinulović, Katarina",
year = "2004",
abstract = "The effects of some Pd(II) complexes on Na,K-ATPase were studied by kinetic analysis. Na,K-ATPase obeyed Michaelis-Menten kinetics in the absence and presence of [PdCl4] 2-, [Pd(dien)Cl]+  and [Pd(Me4dien)Cl]+ . The kinetic parameters (Km and Vmax) showed that Pd(II) complexes are noncompetitive inhibitors of Na,K-ATPase. Based on the values of inhibitor constants (Ki) determined from Dixon plots, we concluded that Pd(II) complex potency to inhibit the Na,K-ATPase activity depends on steric bulkness of its ligands.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry",
title = "The mechanism of interference of some Pd(II) complexes with Na,K-ATPase activity - kinetic analysis",
volume = "1",
pages = "237-239",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9489"
}

Krinulović, K.. (2004). The mechanism of interference of some Pd(II) complexes with Na,K-ATPase activity - kinetic analysis. in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry
Society of Physical Chemists of Serbia., 1, 237-239.
https://hdl.handle.net/21.15107/rcub_vinar_9489

Krinulović K. The mechanism of interference of some Pd(II) complexes with Na,K-ATPase activity - kinetic analysis. in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry. 2004;1:237-239.
https://hdl.handle.net/21.15107/rcub_vinar_9489 .

Krinulović, Katarina, "The mechanism of interference of some Pd(II) complexes with Na,K-ATPase activity - kinetic analysis" in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry, 1 (2004):237-239,
https://hdl.handle.net/21.15107/rcub_vinar_9489 .

TY  - CONF
AU  - Krinulović, Katarina
PY  - 2004
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9487
AB  - The effects of some Pd(II) complexes on Na,K-ATPase activity in the presence and absence of L-cysteine were studied. The aim of the study was to examine the ability of sulphur-donor ligand (L-cysteine) to prevent and recover the Pd(II) complexesinduced inhibition of Na,K-ATPase. The dose-dependent inhibition of Na,K-ATPase activity wasinduced in all cases. The addition of 1 mM L-cysteine to the reaction mixture prevented the inhibition. Moreover, the inhibited enzymatic activity was reversed by L-cysteine in concentration-dependent manner.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry
T1  - Effect of L-cysteine on the inhibition of Na,K-atpase activity in the presence of some Pd(II) complexes
VL  - 1
SP  - 231
EP  - 233
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9487
ER  - 

@conference{
author = "Krinulović, Katarina",
year = "2004",
abstract = "The effects of some Pd(II) complexes on Na,K-ATPase activity in the presence and absence of L-cysteine were studied. The aim of the study was to examine the ability of sulphur-donor ligand (L-cysteine) to prevent and recover the Pd(II) complexesinduced inhibition of Na,K-ATPase. The dose-dependent inhibition of Na,K-ATPase activity wasinduced in all cases. The addition of 1 mM L-cysteine to the reaction mixture prevented the inhibition. Moreover, the inhibited enzymatic activity was reversed by L-cysteine in concentration-dependent manner.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry",
title = "Effect of L-cysteine on the inhibition of Na,K-atpase activity in the presence of some Pd(II) complexes",
volume = "1",
pages = "231-233",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9487"
}

Krinulović, K.. (2004). Effect of L-cysteine on the inhibition of Na,K-atpase activity in the presence of some Pd(II) complexes. in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry
Society of Physical Chemists of Serbia., 1, 231-233.
https://hdl.handle.net/21.15107/rcub_vinar_9487

Krinulović K. Effect of L-cysteine on the inhibition of Na,K-atpase activity in the presence of some Pd(II) complexes. in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry. 2004;1:231-233.
https://hdl.handle.net/21.15107/rcub_vinar_9487 .

Krinulović, Katarina, "Effect of L-cysteine on the inhibition of Na,K-atpase activity in the presence of some Pd(II) complexes" in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry, 1 (2004):231-233,
https://hdl.handle.net/21.15107/rcub_vinar_9487 .