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  - 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
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"
}

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.

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..

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.

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
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"
}

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.

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..

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.

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  - 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
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"
}

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.

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

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.