TY  - JOUR
AU  - Čolović, Mirjana B.
AU  - Krstić, Danijela Z.
AU  - Petrović, Sandra
AU  - Leskovac, Andreja
AU  - Joksić, Gordana
AU  - Savić, Jasmina
AU  - Franko, Mladen
AU  - Trebše, Polonca
AU  - Vasić, Vesna M.
PY  - 2010
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3931
AB  - The toxic effects of diazinon and its irradiated Solutions were investigated using cultivated human blood cells (lymphocytes and erythrocytes) and skin fibroblasts. Ultra Performance Liquid Chromatography (UPLC)-UV/VIS system was used to monitor the disappearance of starting diazinon during 115-min photodegradation and formation of its by-products (diazoxon and 2-isopropyl-6-methyl-4-pyrimidinol (IMP)) as a function of time Dose-dependent AChE and Na+/K+-ATPase inhibition by diazinon was obtained for all investigated cells Calculated IC50 (72 h) values, in M, were 7 5 x 10(-6)/3 4 x 10(-5), 8.7 x 10(-5)/6.6 x 10(-5), and 3 0 x 10(-5)/4 6 x 10(-5) for fibroblast, erythrocyte and lymphocyte AChE/Na+/K+-ATPase, respectively. Results obtained for reference commercially purified target enzymes indicate similar sensitivity of AChE towards diazinon (IC50 (20 min)-7.8 x 10(-5) M). while diazinon concentrations below 10 mM did not noticeably affect Na+/K+-ATPase activity Besides, diazinon and IMP induced increasing incidence of micronuclei (via clastogenic mode of action) in a dose-dependent manner up to 2 x 10(-6) M and significant inhibition of cell proliferation and increased level of malondialdehyde at all investigated concentrations Although after 15-min diazinon irradiation formed products do not affect purified commercial enzymes activities, inhibitory effect of irradiated solutions on cell enzymes increased as a function of time exposure to UV light and resulted in significant reduction of AChE (LIP to 28-45%) and Na+/K+-ATPase (up to 35-40%) at the end of irradiation period Moreover, photodegradation treatment strengthened prooxidative properties of diazinon as well as its potency to induce cytogenetic damage (C) 2009 Elsevier Ireland Ltd All rights reserved.
T2  - Toxicology Letters
T1  - Toxic effects of diazinon and its photodegradation products
VL  - 193
IS  - 1
SP  - 9
EP  - 18
DO  - 10.1016/j.toxlet.2009.11.022
ER  - 

@article{
author = "Čolović, Mirjana B. and Krstić, Danijela Z. and Petrović, Sandra and Leskovac, Andreja and Joksić, Gordana and Savić, Jasmina and Franko, Mladen and Trebše, Polonca and Vasić, Vesna M.",
year = "2010",
abstract = "The toxic effects of diazinon and its irradiated Solutions were investigated using cultivated human blood cells (lymphocytes and erythrocytes) and skin fibroblasts. Ultra Performance Liquid Chromatography (UPLC)-UV/VIS system was used to monitor the disappearance of starting diazinon during 115-min photodegradation and formation of its by-products (diazoxon and 2-isopropyl-6-methyl-4-pyrimidinol (IMP)) as a function of time Dose-dependent AChE and Na+/K+-ATPase inhibition by diazinon was obtained for all investigated cells Calculated IC50 (72 h) values, in M, were 7 5 x 10(-6)/3 4 x 10(-5), 8.7 x 10(-5)/6.6 x 10(-5), and 3 0 x 10(-5)/4 6 x 10(-5) for fibroblast, erythrocyte and lymphocyte AChE/Na+/K+-ATPase, respectively. Results obtained for reference commercially purified target enzymes indicate similar sensitivity of AChE towards diazinon (IC50 (20 min)-7.8 x 10(-5) M). while diazinon concentrations below 10 mM did not noticeably affect Na+/K+-ATPase activity Besides, diazinon and IMP induced increasing incidence of micronuclei (via clastogenic mode of action) in a dose-dependent manner up to 2 x 10(-6) M and significant inhibition of cell proliferation and increased level of malondialdehyde at all investigated concentrations Although after 15-min diazinon irradiation formed products do not affect purified commercial enzymes activities, inhibitory effect of irradiated solutions on cell enzymes increased as a function of time exposure to UV light and resulted in significant reduction of AChE (LIP to 28-45%) and Na+/K+-ATPase (up to 35-40%) at the end of irradiation period Moreover, photodegradation treatment strengthened prooxidative properties of diazinon as well as its potency to induce cytogenetic damage (C) 2009 Elsevier Ireland Ltd All rights reserved.",
journal = "Toxicology Letters",
title = "Toxic effects of diazinon and its photodegradation products",
volume = "193",
number = "1",
pages = "9-18",
doi = "10.1016/j.toxlet.2009.11.022"
}

Čolović, M. B., Krstić, D. Z., Petrović, S., Leskovac, A., Joksić, G., Savić, J., Franko, M., Trebše, P.,& Vasić, V. M.. (2010). Toxic effects of diazinon and its photodegradation products. in Toxicology Letters, 193(1), 9-18.
https://doi.org/10.1016/j.toxlet.2009.11.022

Čolović MB, Krstić DZ, Petrović S, Leskovac A, Joksić G, Savić J, Franko M, Trebše P, Vasić VM. Toxic effects of diazinon and its photodegradation products. in Toxicology Letters. 2010;193(1):9-18.
doi:10.1016/j.toxlet.2009.11.022 .

Čolović, Mirjana B., Krstić, Danijela Z., Petrović, Sandra, Leskovac, Andreja, Joksić, Gordana, Savić, Jasmina, Franko, Mladen, Trebše, Polonca, Vasić, Vesna M., "Toxic effects of diazinon and its photodegradation products" in Toxicology Letters, 193, no. 1 (2010):9-18,
https://doi.org/10.1016/j.toxlet.2009.11.022 . .

TY  - JOUR
AU  - Petković, Marijana
AU  - Petrović, Biljana
AU  - Savić, Jasmina
AU  - Bugarčić, Živadin D.
AU  - Dimitrić-Marković, Jasmina
AU  - Momić, Tatjana
AU  - Vasić, Vesna M.
PY  - 2010
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3909
AB  - Matrix-assisted laser desorption and ionization time-of-flight mass spectrometry (MALDI-TOF MS) is a suitable method for the analysis of inorganic and organic compounds and biomolecules This makes. MALDI-TOF MS convenient for monitoring the interaction of metallo-drugs with biomolecules. Results presented in this manuscript demonstrate that flavonoids such as apigenin, kaempferol and luteolin are suitable for MALDI-TOF MS analysis of Pt(II), Pd(II), Pt(IV) and Ru(III) complexes, giving different signal-to-noise ratios of the analyte peak. The MALDI-TOF mass spectra of inorganic complexes acquired with these flavonoid matrices are easy to interpret and have some advantages over the application of other commonly used matrices: a low number of matrix peaks are detectable and the coordinative metal-ligand bond is, in most cases, preserved. On the other hand, flavonoids do not act as typical matrices, as their excess is not required for the acquisition of MALDI-TOF mass spectra of inorganic complexes. (C) 2009 Elsevier B.V. All rights reserved.
T2  - International Journal of Mass Spectrometry
T1  - Flavonoids as matrices for MALDI-TOF mass spectrometric analysis of transition metal complexes
VL  - 290
IS  - 1
SP  - 39
EP  - 46
DO  - 10.1016/j.ijms.2009.12.001
ER  - 

@article{
author = "Petković, Marijana and Petrović, Biljana and Savić, Jasmina and Bugarčić, Živadin D. and Dimitrić-Marković, Jasmina and Momić, Tatjana and Vasić, Vesna M.",
year = "2010",
abstract = "Matrix-assisted laser desorption and ionization time-of-flight mass spectrometry (MALDI-TOF MS) is a suitable method for the analysis of inorganic and organic compounds and biomolecules This makes. MALDI-TOF MS convenient for monitoring the interaction of metallo-drugs with biomolecules. Results presented in this manuscript demonstrate that flavonoids such as apigenin, kaempferol and luteolin are suitable for MALDI-TOF MS analysis of Pt(II), Pd(II), Pt(IV) and Ru(III) complexes, giving different signal-to-noise ratios of the analyte peak. The MALDI-TOF mass spectra of inorganic complexes acquired with these flavonoid matrices are easy to interpret and have some advantages over the application of other commonly used matrices: a low number of matrix peaks are detectable and the coordinative metal-ligand bond is, in most cases, preserved. On the other hand, flavonoids do not act as typical matrices, as their excess is not required for the acquisition of MALDI-TOF mass spectra of inorganic complexes. (C) 2009 Elsevier B.V. All rights reserved.",
journal = "International Journal of Mass Spectrometry",
title = "Flavonoids as matrices for MALDI-TOF mass spectrometric analysis of transition metal complexes",
volume = "290",
number = "1",
pages = "39-46",
doi = "10.1016/j.ijms.2009.12.001"
}

Petković, M., Petrović, B., Savić, J., Bugarčić, Ž. D., Dimitrić-Marković, J., Momić, T.,& Vasić, V. M.. (2010). Flavonoids as matrices for MALDI-TOF mass spectrometric analysis of transition metal complexes. in International Journal of Mass Spectrometry, 290(1), 39-46.
https://doi.org/10.1016/j.ijms.2009.12.001

Petković M, Petrović B, Savić J, Bugarčić ŽD, Dimitrić-Marković J, Momić T, Vasić VM. Flavonoids as matrices for MALDI-TOF mass spectrometric analysis of transition metal complexes. in International Journal of Mass Spectrometry. 2010;290(1):39-46.
doi:10.1016/j.ijms.2009.12.001 .

Petković, Marijana, Petrović, Biljana, Savić, Jasmina, Bugarčić, Živadin D., Dimitrić-Marković, Jasmina, Momić, Tatjana, Vasić, Vesna M., "Flavonoids as matrices for MALDI-TOF mass spectrometric analysis of transition metal complexes" in International Journal of Mass Spectrometry, 290, no. 1 (2010):39-46,
https://doi.org/10.1016/j.ijms.2009.12.001 . .

TY  - CONF
AU  - Damnjanović, Bojana
AU  - Petrović, Biljana
AU  - Dimitrić Marković, Jasmina
AU  - Petković, Marijana
PY  - 2010
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9287
AB  - In this work, we have analyzed the positive ion MALDI-TOF mass spectra of cationic
complexes [PdCl(dien)]Cl and [Ru(en)2Cl2]Cl acquired with different matrices: 2,5-
dihydroxybenzoic acid (DHB), α-cyano hydroxycinnamic acid (CHCA) and quercetin.
The necessity to test several matrix/analyte combinations for reliable identification and
characterization of metallo-drugs is emphasized in this work.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2010 : 10th international conference on fundamental and applied aspects of physical chemistry
T1  - Maldi-tof ms characterization of transition metal complexes
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9287
ER  - 

@conference{
author = "Damnjanović, Bojana and Petrović, Biljana and Dimitrić Marković, Jasmina and Petković, Marijana",
year = "2010",
abstract = "In this work, we have analyzed the positive ion MALDI-TOF mass spectra of cationic
complexes [PdCl(dien)]Cl and [Ru(en)2Cl2]Cl acquired with different matrices: 2,5-
dihydroxybenzoic acid (DHB), α-cyano hydroxycinnamic acid (CHCA) and quercetin.
The necessity to test several matrix/analyte combinations for reliable identification and
characterization of metallo-drugs is emphasized in this work.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2010 : 10th international conference on fundamental and applied aspects of physical chemistry",
title = "Maldi-tof ms characterization of transition metal complexes",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9287"
}

Damnjanović, B., Petrović, B., Dimitrić Marković, J.,& Petković, M.. (2010). Maldi-tof ms characterization of transition metal complexes. in Physical chemistry 2010 : 10th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia..
https://hdl.handle.net/21.15107/rcub_vinar_9287

Damnjanović B, Petrović B, Dimitrić Marković J, Petković M. Maldi-tof ms characterization of transition metal complexes. in Physical chemistry 2010 : 10th international conference on fundamental and applied aspects of physical chemistry. 2010;.
https://hdl.handle.net/21.15107/rcub_vinar_9287 .

Damnjanović, Bojana, Petrović, Biljana, Dimitrić Marković, Jasmina, Petković, Marijana, "Maldi-tof ms characterization of transition metal complexes" in Physical chemistry 2010 : 10th international conference on fundamental and applied aspects of physical chemistry (2010),
https://hdl.handle.net/21.15107/rcub_vinar_9287 .

TY  - JOUR
AU  - Vasić, Vesna M.
AU  - Čolović, Mirjana B.
AU  - Krstić, Danijela Z.
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3895
AB  - The aim of the study was to give an overview of the mechanism of inhibition of Na+/K+-ATPase and Mg2+-ATPase activity, the enzymes playing a key role in the active transport of monovalent cations (Na+ and K+) across the cell membrane, induced by the ions of some transition (Cu2+, Zn2+, Fe2+, Co2+) and heavy (Hg2+ i Cd2+) metals, ammonium decavanadate and noble metals complexes ([PtCl2DMSO2], [AuCl4](-), [PdCl4](2-), [PdCl(dien)](+), [PdCl(Me(4)dien)](+)). The extensive kinetic analysis was done in order to determine kinetic parameters and the mode of interaction of Na+/K+-ATPase and Mg2+-ATPase and the investigated compounds. In addition, the ability of sulphur-donor ligands (L-cysteine and glulathione), as well as EDTA, to prevent metal ions and complexes induced inhibition of Na+/K+-ATPase activity and to recover enzymatic activity was investigated Finally, development of highly sensitive and selective analytical tools on the basis of the immobilized enzyme is discussed in this paper.
AB  - U ovom radu je dat pregled mehanizma interakcije Na+/K+–ATPaze i Mg2+–ATPaze, enzima koji igraju ključnu ulogu u aktivnom transportu katjona kroz ćelijsku membranu, i jona prelaznih metala (Cu2+, Zn2+, Fe2+ i Co2+), jona teških metala (Hg2+ i Cd2+), amonijum-dekavanadata i kompleksa plemenitih metala ([PtCl2DMSO2], [AuCl4]–, [PdCl4]2–, [PdCl(dien)]+, [PdCl(Me4dien)]+). Kinetička analiza je urađena u cilju određivanja kinetičkih parametara i tipa inhibicije enzima ovim jedinjenjima. Takođe je ispitivana sposobnost L-cisteina i glutationa (koji sadrže sumpor) da spreče inhibiciju Na+/K+–ATPaze matalnim jonima i kompleksima plemenitih metala i reaktiviraju aktivnost inhibiranog enzima. Na kraju, razvoj osetljivih i selektivnih analitičkih oruđa na bazi imobilizovane Na+/K+––ATPaze je razmotren.
T2  - Hemijska industrija
T1  - Mechanism of Na+/K+-Atpase and Mg2+-Atpase Inhibition By Metal Ions and Complexes
T1  - Mehanizam inhibicije Na+/K+–ATPaze i Mg2+–ATPaze metalnim jonima i kompleksima
VL  - 63
IS  - 5a
SP  - 499
EP  - 509
DO  - 10.2298/HEMIND0905499V
ER  - 

@article{
author = "Vasić, Vesna M. and Čolović, Mirjana B. and Krstić, Danijela Z.",
year = "2009",
abstract = "The aim of the study was to give an overview of the mechanism of inhibition of Na+/K+-ATPase and Mg2+-ATPase activity, the enzymes playing a key role in the active transport of monovalent cations (Na+ and K+) across the cell membrane, induced by the ions of some transition (Cu2+, Zn2+, Fe2+, Co2+) and heavy (Hg2+ i Cd2+) metals, ammonium decavanadate and noble metals complexes ([PtCl2DMSO2], [AuCl4](-), [PdCl4](2-), [PdCl(dien)](+), [PdCl(Me(4)dien)](+)). The extensive kinetic analysis was done in order to determine kinetic parameters and the mode of interaction of Na+/K+-ATPase and Mg2+-ATPase and the investigated compounds. In addition, the ability of sulphur-donor ligands (L-cysteine and glulathione), as well as EDTA, to prevent metal ions and complexes induced inhibition of Na+/K+-ATPase activity and to recover enzymatic activity was investigated Finally, development of highly sensitive and selective analytical tools on the basis of the immobilized enzyme is discussed in this paper., U ovom radu je dat pregled mehanizma interakcije Na+/K+–ATPaze i Mg2+–ATPaze, enzima koji igraju ključnu ulogu u aktivnom transportu katjona kroz ćelijsku membranu, i jona prelaznih metala (Cu2+, Zn2+, Fe2+ i Co2+), jona teških metala (Hg2+ i Cd2+), amonijum-dekavanadata i kompleksa plemenitih metala ([PtCl2DMSO2], [AuCl4]–, [PdCl4]2–, [PdCl(dien)]+, [PdCl(Me4dien)]+). Kinetička analiza je urađena u cilju određivanja kinetičkih parametara i tipa inhibicije enzima ovim jedinjenjima. Takođe je ispitivana sposobnost L-cisteina i glutationa (koji sadrže sumpor) da spreče inhibiciju Na+/K+–ATPaze matalnim jonima i kompleksima plemenitih metala i reaktiviraju aktivnost inhibiranog enzima. Na kraju, razvoj osetljivih i selektivnih analitičkih oruđa na bazi imobilizovane Na+/K+––ATPaze je razmotren.",
journal = "Hemijska industrija",
title = "Mechanism of Na+/K+-Atpase and Mg2+-Atpase Inhibition By Metal Ions and Complexes, Mehanizam inhibicije Na+/K+–ATPaze i Mg2+–ATPaze metalnim jonima i kompleksima",
volume = "63",
number = "5a",
pages = "499-509",
doi = "10.2298/HEMIND0905499V"
}

Vasić, V. M., Čolović, M. B.,& Krstić, D. Z.. (2009). Mechanism of Na+/K+-Atpase and Mg2+-Atpase Inhibition By Metal Ions and Complexes. in Hemijska industrija, 63(5a), 499-509.
https://doi.org/10.2298/HEMIND0905499V

Vasić VM, Čolović MB, Krstić DZ. Mechanism of Na+/K+-Atpase and Mg2+-Atpase Inhibition By Metal Ions and Complexes. in Hemijska industrija. 2009;63(5a):499-509.
doi:10.2298/HEMIND0905499V .

Vasić, Vesna M., Čolović, Mirjana B., Krstić, Danijela Z., "Mechanism of Na+/K+-Atpase and Mg2+-Atpase Inhibition By Metal Ions and Complexes" in Hemijska industrija, 63, no. 5a (2009):499-509,
https://doi.org/10.2298/HEMIND0905499V . .

TY  - JOUR
AU  - Krstić, Danijela Z.
AU  - Čolović, Mirjana B.
AU  - Bošnjaković-Pavlović, Nada
AU  - Spasojević-de Bire, Anne
AU  - Vasić, Vesna M.
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3840
AB  - The in vitro influence of decameric vanadate species on Na(+)/K(+)-ATPase, plasma membrane Ca(2+)-ATPase (PMCA)-calcium pump and ecto-ATPase activity, using rat synaptic plasma membrane (SPM) as model system was investigated, whereas the commercial porcine cerebral cortex Na(+)/K(+)-ATPase served as a reference. The thermal behaviour of the synthesized decavanadate (V(10)) has been studied by differential scanning calorimetry and thermogravimetric analysis, while the type of polyvanadate anion was identified using the IR spectroscopy. The concentration-dependent responses to V(10) of all enzymes were obtained. The half-maximum inhibitory concentration (IC(50)) of the enzyme activity was achieved at (4.74 +/- 1.15) x 10(-7) mol/l for SPM Na(+)/K(+)-ATPase, (1.30 +/- 0.10) x 10(-6) mol/l for commercial Na(+)/K(+)-ATPase and (3.13 +/- 1.70) x 10(-8) mol/l for Ca(2+)-ATPase, while ecto-ATPase is significantly less sensitive toward V(10) (IC(50) = (1.05 +/- 0.10) x 10(-4) mol/l) than investigated P-type ATPases. Kinetic analysis showed that V(10) inhibited Na(+)/K(+)-ATPase by reducing the maximum enzymatic velocity and apparent affinity for ATP (increasing K(m) value), implying a mixed mode of interaction between V(10) and P-type ATPases.
T2  - General Physiology and Biophysics
T1  - Influence of decavanadate on rat synaptic plasma membrane ATPases activity
VL  - 28
IS  - 3
SP  - 302
EP  - 308
DO  - 10.4149/gpb_2009_03_302
ER  - 

@article{
author = "Krstić, Danijela Z. and Čolović, Mirjana B. and Bošnjaković-Pavlović, Nada and Spasojević-de Bire, Anne and Vasić, Vesna M.",
year = "2009",
abstract = "The in vitro influence of decameric vanadate species on Na(+)/K(+)-ATPase, plasma membrane Ca(2+)-ATPase (PMCA)-calcium pump and ecto-ATPase activity, using rat synaptic plasma membrane (SPM) as model system was investigated, whereas the commercial porcine cerebral cortex Na(+)/K(+)-ATPase served as a reference. The thermal behaviour of the synthesized decavanadate (V(10)) has been studied by differential scanning calorimetry and thermogravimetric analysis, while the type of polyvanadate anion was identified using the IR spectroscopy. The concentration-dependent responses to V(10) of all enzymes were obtained. The half-maximum inhibitory concentration (IC(50)) of the enzyme activity was achieved at (4.74 +/- 1.15) x 10(-7) mol/l for SPM Na(+)/K(+)-ATPase, (1.30 +/- 0.10) x 10(-6) mol/l for commercial Na(+)/K(+)-ATPase and (3.13 +/- 1.70) x 10(-8) mol/l for Ca(2+)-ATPase, while ecto-ATPase is significantly less sensitive toward V(10) (IC(50) = (1.05 +/- 0.10) x 10(-4) mol/l) than investigated P-type ATPases. Kinetic analysis showed that V(10) inhibited Na(+)/K(+)-ATPase by reducing the maximum enzymatic velocity and apparent affinity for ATP (increasing K(m) value), implying a mixed mode of interaction between V(10) and P-type ATPases.",
journal = "General Physiology and Biophysics",
title = "Influence of decavanadate on rat synaptic plasma membrane ATPases activity",
volume = "28",
number = "3",
pages = "302-308",
doi = "10.4149/gpb_2009_03_302"
}

Krstić, D. Z., Čolović, M. B., Bošnjaković-Pavlović, N., Spasojević-de Bire, A.,& Vasić, V. M.. (2009). Influence of decavanadate on rat synaptic plasma membrane ATPases activity. in General Physiology and Biophysics, 28(3), 302-308.
https://doi.org/10.4149/gpb_2009_03_302

Krstić DZ, Čolović MB, Bošnjaković-Pavlović N, Spasojević-de Bire A, Vasić VM. Influence of decavanadate on rat synaptic plasma membrane ATPases activity. in General Physiology and Biophysics. 2009;28(3):302-308.
doi:10.4149/gpb_2009_03_302 .

Krstić, Danijela Z., Čolović, Mirjana B., Bošnjaković-Pavlović, Nada, Spasojević-de Bire, Anne, Vasić, Vesna M., "Influence of decavanadate on rat synaptic plasma membrane ATPases activity" in General Physiology and Biophysics, 28, no. 3 (2009):302-308,
https://doi.org/10.4149/gpb_2009_03_302 . .

TY  - JOUR
AU  - Vasić, Dragana D.
AU  - Savić, Jasmina
AU  - Bugaricic, Zivadin
AU  - Krstić, Danijela Z.
AU  - Tomić, Nenad
AU  - Čolović, Mirjana B.
AU  - Petković, Marijana
AU  - Vasić, Vesna M.
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3657
AB  - The reaction between [PtCl,(DMSO)(2)] and L-cysteine (L-Cys) has been investigated in the presence of micelles of sodium dodecyl sulfate (SDS) - as a model for biological membranes. Additionally, the inhibitory effect of [PtCl2(DMSO)(2)] on the Na+,K+-ATPise activity and its partial prevention with 10 mM L-Cys were demonstrated. The interaction of L-Cys with [Ptcl(2)(DMSO)(2)] resulted in the formation of a [Pt(DMSO)(2)L-Cys)(2)](2+) (DMSO)(2)] Complex, which most probably occurs through stepwise replacement of Cl- with L-Cys. It has also been demonstrated that neither the pH value nor SDS affects the composition of the new complex. On the other hand, the pH value and SDS do affect the reaction rate, most probably due to electrostatic interactions with reactants. In Summary, this study can be used as a simple model approach for the investigation of reaction mechanisms between platinum complexes and various biomolecules, and for the determination of potential toxicity and/or side effects of antitumour platinum drugs.
T2  - Zeitschrift fur Naturforschung. Section C: Journal of Biosciences
T1  - Interaction of the [PtCl2(DMSO)(2)] Complex with L-Cysteine
VL  - 64
IS  - 1-2
SP  - 103
EP  - 108
DO  - 10.1515/znc-2009-1-217
UR  - https://hdl.handle.net/21.15107/rcub_vinar_3657
ER  - 

@article{
author = "Vasić, Dragana D. and Savić, Jasmina and Bugaricic, Zivadin and Krstić, Danijela Z. and Tomić, Nenad and Čolović, Mirjana B. and Petković, Marijana and Vasić, Vesna M.",
year = "2009",
abstract = "The reaction between [PtCl,(DMSO)(2)] and L-cysteine (L-Cys) has been investigated in the presence of micelles of sodium dodecyl sulfate (SDS) - as a model for biological membranes. Additionally, the inhibitory effect of [PtCl2(DMSO)(2)] on the Na+,K+-ATPise activity and its partial prevention with 10 mM L-Cys were demonstrated. The interaction of L-Cys with [Ptcl(2)(DMSO)(2)] resulted in the formation of a [Pt(DMSO)(2)L-Cys)(2)](2+) (DMSO)(2)] Complex, which most probably occurs through stepwise replacement of Cl- with L-Cys. It has also been demonstrated that neither the pH value nor SDS affects the composition of the new complex. On the other hand, the pH value and SDS do affect the reaction rate, most probably due to electrostatic interactions with reactants. In Summary, this study can be used as a simple model approach for the investigation of reaction mechanisms between platinum complexes and various biomolecules, and for the determination of potential toxicity and/or side effects of antitumour platinum drugs.",
journal = "Zeitschrift fur Naturforschung. Section C: Journal of Biosciences",
title = "Interaction of the [PtCl2(DMSO)(2)] Complex with L-Cysteine",
volume = "64",
number = "1-2",
pages = "103-108",
doi = "10.1515/znc-2009-1-217",
url = "https://hdl.handle.net/21.15107/rcub_vinar_3657"
}

Vasić, D. D., Savić, J., Bugaricic, Z., Krstić, D. Z., Tomić, N., Čolović, M. B., Petković, M.,& Vasić, V. M.. (2009). Interaction of the [PtCl2(DMSO)(2)] Complex with L-Cysteine. in Zeitschrift fur Naturforschung. Section C: Journal of Biosciences, 64(1-2), 103-108.
https://doi.org/10.1515/znc-2009-1-217
https://hdl.handle.net/21.15107/rcub_vinar_3657

Vasić DD, Savić J, Bugaricic Z, Krstić DZ, Tomić N, Čolović MB, Petković M, Vasić VM. Interaction of the [PtCl2(DMSO)(2)] Complex with L-Cysteine. in Zeitschrift fur Naturforschung. Section C: Journal of Biosciences. 2009;64(1-2):103-108.
doi:10.1515/znc-2009-1-217
https://hdl.handle.net/21.15107/rcub_vinar_3657 .

Vasić, Dragana D., Savić, Jasmina, Bugaricic, Zivadin, Krstić, Danijela Z., Tomić, Nenad, Čolović, Mirjana B., Petković, Marijana, Vasić, Vesna M., "Interaction of the [PtCl2(DMSO)(2)] Complex with L-Cysteine" in Zeitschrift fur Naturforschung. Section C: Journal of Biosciences, 64, no. 1-2 (2009):103-108,
https://doi.org/10.1515/znc-2009-1-217 .,
https://hdl.handle.net/21.15107/rcub_vinar_3657 .

TY  - JOUR
AU  - Cojocaru, Corneliu
AU  - Diaconu, Mariana
AU  - Cretescu, Igor
AU  - Savić, Jasmina
AU  - Vasić, Vesna M.
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3636
AB  - The ability of dried yeast Saccharomyces biomass to remove Cu(II) ions from aqueous solutions was investigated by using of batch techniques. The influence of different parameters on copper uptake by dried yeast, such as initial Cu(II) concentration, initial pH of solution and temperature, was studied. The Freundlich, Langmuir, Redlich-Peterson and Sips isotherms were applied to the obtained experimental data. According to Langmuir isotherm the maximum adsorption capacity of investigated non-living biomass was found to be 2.59 mg/g. The thermodynamic parameters (e.g. free energy and enthalpy) were calculated and discussed. The adsorption of Cu(II) onto the dried cells of Saccharomyces cerevisiae is an endothermic process and become more favorable with the increasing of temperature in pH range from 3 to 4. Optimization studies by means of response surface methodology were carried out, which resulted in improvement of the efficiency of sorption removal by using of biomass. The removal efficiency of real wastewater originating from electroplating industry which contains Sn(II) ions was determined and compared with synthetic wastewater obtained in laboratory. (C) 2008 Elsevier B.V. All rights reserved.
T2  - Colloids and Surfaces. A: Physicochemical and Engineering Aspects
T1  - Biosorption of copper(II) ions from aqua solutions using dried yeast biomass
VL  - 335
IS  - 1-3
SP  - 181
EP  - 188
DO  - 10.1016/j.colsurfa.2008.11.003
ER  - 

@article{
author = "Cojocaru, Corneliu and Diaconu, Mariana and Cretescu, Igor and Savić, Jasmina and Vasić, Vesna M.",
year = "2009",
abstract = "The ability of dried yeast Saccharomyces biomass to remove Cu(II) ions from aqueous solutions was investigated by using of batch techniques. The influence of different parameters on copper uptake by dried yeast, such as initial Cu(II) concentration, initial pH of solution and temperature, was studied. The Freundlich, Langmuir, Redlich-Peterson and Sips isotherms were applied to the obtained experimental data. According to Langmuir isotherm the maximum adsorption capacity of investigated non-living biomass was found to be 2.59 mg/g. The thermodynamic parameters (e.g. free energy and enthalpy) were calculated and discussed. The adsorption of Cu(II) onto the dried cells of Saccharomyces cerevisiae is an endothermic process and become more favorable with the increasing of temperature in pH range from 3 to 4. Optimization studies by means of response surface methodology were carried out, which resulted in improvement of the efficiency of sorption removal by using of biomass. The removal efficiency of real wastewater originating from electroplating industry which contains Sn(II) ions was determined and compared with synthetic wastewater obtained in laboratory. (C) 2008 Elsevier B.V. All rights reserved.",
journal = "Colloids and Surfaces. A: Physicochemical and Engineering Aspects",
title = "Biosorption of copper(II) ions from aqua solutions using dried yeast biomass",
volume = "335",
number = "1-3",
pages = "181-188",
doi = "10.1016/j.colsurfa.2008.11.003"
}

Cojocaru, C., Diaconu, M., Cretescu, I., Savić, J.,& Vasić, V. M.. (2009). Biosorption of copper(II) ions from aqua solutions using dried yeast biomass. in Colloids and Surfaces. A: Physicochemical and Engineering Aspects, 335(1-3), 181-188.
https://doi.org/10.1016/j.colsurfa.2008.11.003

Cojocaru C, Diaconu M, Cretescu I, Savić J, Vasić VM. Biosorption of copper(II) ions from aqua solutions using dried yeast biomass. in Colloids and Surfaces. A: Physicochemical and Engineering Aspects. 2009;335(1-3):181-188.
doi:10.1016/j.colsurfa.2008.11.003 .

Cojocaru, Corneliu, Diaconu, Mariana, Cretescu, Igor, Savić, Jasmina, Vasić, Vesna M., "Biosorption of copper(II) ions from aqua solutions using dried yeast biomass" in Colloids and Surfaces. A: Physicochemical and Engineering Aspects, 335, no. 1-3 (2009):181-188,
https://doi.org/10.1016/j.colsurfa.2008.11.003 . .

TY  - JOUR
AU  - Vujačić, Ana V.
AU  - Savić, Jasmina
AU  - Sovilj, Sofija P.
AU  - Szecsenyi, K. Meszaros
AU  - Todorović, N.
AU  - Petković, Marijana
AU  - Vasić, Vesna M.
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3653
AB  - The kinetics of the reaction between the tetrachloroaurate(III) ion and L-methionine (L-Met) (0.1 M HClO4, pH 1.0-2.5) have been studied spectrophotometrically using a stopped-flow technique at different temperatures. Initially, the fast substitution reaction was ascribed to the formation of the short-lived square-planar Au(III)-(L-Met) that was followed by the replacement of a Cl- ligand and a subsequent, slower reduction to Au(I)-(L-Met). This is an intermolecular process, involving attack on the [AuCl4](-) Complex by an outer-sphere L-methionine. The activation parameters (Delta H-not equal and Delta S-not equal) for substitution and reduction were determined. IR spectroscopy indicates that L-methionine acts as a bidentate ligand, most likely coordinating via the S and N atoms, while H-1 and C-13 NMR data indicate methionine sulfoxide as the final product. Finally, the components of the reaction were treated thermally in order to investigate the solid phase synthesis of the resulting complex. (C) 2008 Elsevier Ltd. All rights reserved.
T2  - Polyhedron
T1  - Mechanism of complex formation between [AuCl4](-) and L-methionine
VL  - 28
IS  - 3
SP  - 593
EP  - 599
DO  - 10.1016/j.poly.2008.11.045
ER  - 

@article{
author = "Vujačić, Ana V. and Savić, Jasmina and Sovilj, Sofija P. and Szecsenyi, K. Meszaros and Todorović, N. and Petković, Marijana and Vasić, Vesna M.",
year = "2009",
abstract = "The kinetics of the reaction between the tetrachloroaurate(III) ion and L-methionine (L-Met) (0.1 M HClO4, pH 1.0-2.5) have been studied spectrophotometrically using a stopped-flow technique at different temperatures. Initially, the fast substitution reaction was ascribed to the formation of the short-lived square-planar Au(III)-(L-Met) that was followed by the replacement of a Cl- ligand and a subsequent, slower reduction to Au(I)-(L-Met). This is an intermolecular process, involving attack on the [AuCl4](-) Complex by an outer-sphere L-methionine. The activation parameters (Delta H-not equal and Delta S-not equal) for substitution and reduction were determined. IR spectroscopy indicates that L-methionine acts as a bidentate ligand, most likely coordinating via the S and N atoms, while H-1 and C-13 NMR data indicate methionine sulfoxide as the final product. Finally, the components of the reaction were treated thermally in order to investigate the solid phase synthesis of the resulting complex. (C) 2008 Elsevier Ltd. All rights reserved.",
journal = "Polyhedron",
title = "Mechanism of complex formation between [AuCl4](-) and L-methionine",
volume = "28",
number = "3",
pages = "593-599",
doi = "10.1016/j.poly.2008.11.045"
}

Vujačić, A. V., Savić, J., Sovilj, S. P., Szecsenyi, K. M., Todorović, N., Petković, M.,& Vasić, V. M.. (2009). Mechanism of complex formation between [AuCl4](-) and L-methionine. in Polyhedron, 28(3), 593-599.
https://doi.org/10.1016/j.poly.2008.11.045

Vujačić AV, Savić J, Sovilj SP, Szecsenyi KM, Todorović N, Petković M, Vasić VM. Mechanism of complex formation between [AuCl4](-) and L-methionine. in Polyhedron. 2009;28(3):593-599.
doi:10.1016/j.poly.2008.11.045 .

Vujačić, Ana V., Savić, Jasmina, Sovilj, Sofija P., Szecsenyi, K. Meszaros, Todorović, N., Petković, Marijana, Vasić, Vesna M., "Mechanism of complex formation between [AuCl4](-) and L-methionine" in Polyhedron, 28, no. 3 (2009):593-599,
https://doi.org/10.1016/j.poly.2008.11.045 . .

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  - CONF
AU  - Savić, Jasmina
AU  - Momić, Tatjana
AU  - Milenković, Aleksandra S.
AU  - Vujačić, Ana V.
AU  - Vasić, Vesna M.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9360
AB  - The equilibrium and kinetics of the reaction between tetrachloroaurate(III) ion (AuCl4 - ) and quercetin in 0.1 M HClO4 were studied spectrophotometrically. The fast and the slow reaction steps were distinguished in the reaction mechanism, depending on the ratio of AuCl4 -  and quercetin concentration. The stoichiometry of reaction, determined by molar ratio and Jobb’s methods, was 1:1. The kinetics of complex formation was followed under the pseudo-first order conditions by measuring the absorbance at 294 nm vs. time as the function of quercetin concentration in 5 – 15 fold excess.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
T1  - Spectrophotometric and uplc study of reaction between [AuCl4] - and quercetin
VL  - 1
SP  - 172
EP  - 174
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9360
ER  - 

@conference{
author = "Savić, Jasmina and Momić, Tatjana and Milenković, Aleksandra S. and Vujačić, Ana V. and Vasić, Vesna M.",
year = "2008",
abstract = "The equilibrium and kinetics of the reaction between tetrachloroaurate(III) ion (AuCl4 - ) and quercetin in 0.1 M HClO4 were studied spectrophotometrically. The fast and the slow reaction steps were distinguished in the reaction mechanism, depending on the ratio of AuCl4 -  and quercetin concentration. The stoichiometry of reaction, determined by molar ratio and Jobb’s methods, was 1:1. The kinetics of complex formation was followed under the pseudo-first order conditions by measuring the absorbance at 294 nm vs. time as the function of quercetin concentration in 5 – 15 fold excess.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry",
title = "Spectrophotometric and uplc study of reaction between [AuCl4] - and quercetin",
volume = "1",
pages = "172-174",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9360"
}

Savić, J., Momić, T., Milenković, A. S., Vujačić, A. V.,& Vasić, V. M.. (2008). Spectrophotometric and uplc study of reaction between [AuCl4] - and quercetin. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia., 1, 172-174.
https://hdl.handle.net/21.15107/rcub_vinar_9360

Savić J, Momić T, Milenković AS, Vujačić AV, Vasić VM. Spectrophotometric and uplc study of reaction between [AuCl4] - and quercetin. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry. 2008;1:172-174.
https://hdl.handle.net/21.15107/rcub_vinar_9360 .

Savić, Jasmina, Momić, Tatjana, Milenković, Aleksandra S., Vujačić, Ana V., Vasić, Vesna M., "Spectrophotometric and uplc study of reaction between [AuCl4] - and quercetin" in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry, 1 (2008):172-174,
https://hdl.handle.net/21.15107/rcub_vinar_9360 .

TY  - CONF
AU  - Vasić, Vesna M.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9365
AB  - The aim of the study was to give an overview of the mechanism of inhibition of Na+/K+-ATPase activity. For this purpose, the effect of ouabain like compounds (digoxin, gitoxin), platinum group complexes ([PdCl4]2-, [PdCl(dien)]+ and [PdCl(Me4dien)]+), transition metal ions (Cu2+, Zn2+, Fe2+, Co2+) and heavy metal ions (Hg2+, Pb2+, Cd2+) on the activity of Na+/K+-ATPase isolated from rat synaptic plasma membranes (SPM), cortex of pig and human erythrocytes and was investigated.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
T1  - Na+/K+-atpase - activity and inhibition
VL  - 1
SP  - 335
EP  - 342
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9365
ER  - 

@conference{
author = "Vasić, Vesna M.",
year = "2008",
abstract = "The aim of the study was to give an overview of the mechanism of inhibition of Na+/K+-ATPase activity. For this purpose, the effect of ouabain like compounds (digoxin, gitoxin), platinum group complexes ([PdCl4]2-, [PdCl(dien)]+ and [PdCl(Me4dien)]+), transition metal ions (Cu2+, Zn2+, Fe2+, Co2+) and heavy metal ions (Hg2+, Pb2+, Cd2+) on the activity of Na+/K+-ATPase isolated from rat synaptic plasma membranes (SPM), cortex of pig and human erythrocytes and was investigated.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry",
title = "Na+/K+-atpase - activity and inhibition",
volume = "1",
pages = "335-342",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9365"
}

Vasić, V. M.. (2008). Na+/K+-atpase - activity and inhibition. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia., 1, 335-342.
https://hdl.handle.net/21.15107/rcub_vinar_9365

Vasić VM. Na+/K+-atpase - activity and inhibition. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry. 2008;1:335-342.
https://hdl.handle.net/21.15107/rcub_vinar_9365 .

Vasić, Vesna M., "Na+/K+-atpase - activity and inhibition" in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry, 1 (2008):335-342,
https://hdl.handle.net/21.15107/rcub_vinar_9365 .

TY  - JOUR
AU  - Vasić, Vesna M.
AU  - Momić, Tatjana
AU  - Petković, Marijana
AU  - Krstić, Danijela Z.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3598
AB  - This paper gives an overview of the literature data concerning specific and non specific inhibitors of Na+,K+-ATPase receptor. The immobilization approaches developed to improve the rather low time and temperature stability of Na+,K+-ATPase, as well to preserve the enzyme properties were overviewed. The functional immobilization of Na+,K+-ATPase receptor as the target, with preservation of the full functional protein activity and access of various substances to an optimum number of binding sites under controlled conditions in the combination with high sensitive technology for the detection of enzyme activity is the basis for application of this enzyme in medical, pharmaceutical and environmental research.
T2  - Sensors
T1  - Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds
VL  - 8
IS  - 12
SP  - 8321
EP  - 8360
DO  - 10.3390/s8128321
ER  - 

@article{
author = "Vasić, Vesna M. and Momić, Tatjana and Petković, Marijana and Krstić, Danijela Z.",
year = "2008",
abstract = "This paper gives an overview of the literature data concerning specific and non specific inhibitors of Na+,K+-ATPase receptor. The immobilization approaches developed to improve the rather low time and temperature stability of Na+,K+-ATPase, as well to preserve the enzyme properties were overviewed. The functional immobilization of Na+,K+-ATPase receptor as the target, with preservation of the full functional protein activity and access of various substances to an optimum number of binding sites under controlled conditions in the combination with high sensitive technology for the detection of enzyme activity is the basis for application of this enzyme in medical, pharmaceutical and environmental research.",
journal = "Sensors",
title = "Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds",
volume = "8",
number = "12",
pages = "8321-8360",
doi = "10.3390/s8128321"
}

Vasić, V. M., Momić, T., Petković, M.,& Krstić, D. Z.. (2008). Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds. in Sensors, 8(12), 8321-8360.
https://doi.org/10.3390/s8128321

Vasić VM, Momić T, Petković M, Krstić DZ. Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds. in Sensors. 2008;8(12):8321-8360.
doi:10.3390/s8128321 .

Vasić, Vesna M., Momić, Tatjana, Petković, Marijana, Krstić, Danijela Z., "Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds" in Sensors, 8, no. 12 (2008):8321-8360,
https://doi.org/10.3390/s8128321 . .

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  - CONF
AU  - Janković, Drina
AU  - Đokić, Divna Đ.
AU  - Nikolić, N.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9384
AB  - In radionuclide therapy, the importance of 90Y as a beta-emitting radionuclide is increasing rapidly. The properties of the 90Y-labeled antimony trisulfide colloid (Sb2S3) were compared with the 99mTc-labeled one. Labeling efficiencies reached >96% and >97% for 90Y- and 99mTc-labeled colloids respectively. Both preparations were stable for 72 h in saline and 1% albumin solution. Filtration analysis showed that more than 94% of total 90Y radioactivity is associated with the colloidal particles smaller than 20 nm, while more than 90% of 99mTc radioactivity is associated with the particles retained on the filter with a 20 nm pore size. 90Y-labeled colloids showed high labeling efficiency, stability and potency for clinical use.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
T1  - Physico-chemical characterization of 90Y-labeled antimony trisulfide colloid and comparison with 99mTc-labeled one
VL  - 2
SP  - 462
EP  - 464
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9384
ER  - 

@conference{
author = "Janković, Drina and Đokić, Divna Đ. and Nikolić, N.",
year = "2008",
abstract = "In radionuclide therapy, the importance of 90Y as a beta-emitting radionuclide is increasing rapidly. The properties of the 90Y-labeled antimony trisulfide colloid (Sb2S3) were compared with the 99mTc-labeled one. Labeling efficiencies reached >96% and >97% for 90Y- and 99mTc-labeled colloids respectively. Both preparations were stable for 72 h in saline and 1% albumin solution. Filtration analysis showed that more than 94% of total 90Y radioactivity is associated with the colloidal particles smaller than 20 nm, while more than 90% of 99mTc radioactivity is associated with the particles retained on the filter with a 20 nm pore size. 90Y-labeled colloids showed high labeling efficiency, stability and potency for clinical use.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry",
title = "Physico-chemical characterization of 90Y-labeled antimony trisulfide colloid and comparison with 99mTc-labeled one",
volume = "2",
pages = "462-464",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9384"
}

Janković, D., Đokić, D. Đ.,& Nikolić, N.. (2008). Physico-chemical characterization of 90Y-labeled antimony trisulfide colloid and comparison with 99mTc-labeled one. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia., 2, 462-464.
https://hdl.handle.net/21.15107/rcub_vinar_9384

Janković D, Đokić DĐ, Nikolić N. Physico-chemical characterization of 90Y-labeled antimony trisulfide colloid and comparison with 99mTc-labeled one. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry. 2008;2:462-464.
https://hdl.handle.net/21.15107/rcub_vinar_9384 .

Janković, Drina, Đokić, Divna Đ., Nikolić, N., "Physico-chemical characterization of 90Y-labeled antimony trisulfide colloid and comparison with 99mTc-labeled one" in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry, 2 (2008):462-464,
https://hdl.handle.net/21.15107/rcub_vinar_9384 .

TY  - JOUR
AU  - Janković, Drina
AU  - Maksin, Tatjana N.
AU  - Đokić, Divna Đ.
AU  - Milonjić, Slobodan K.
AU  - Nikolić, Nadežda S.
AU  - Mirković, Marija D.
AU  - Vranješ-Đurić, Sanja
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3578
AB  - Colloidal particle size is an important characteristic to consider when choosing a radiopharmaceutical for diagnosis and therapeutic purposes in nuclear medicine. Photon correlation spectroscopy (PCS) and transmission electron microscopy (TEM) were used to determine the particle-size distribution of (90)Y- and (99m)Tc-labelled antimony trisulfide (Sb(2)S(3)) and tin colloids (Sn-colloid). (90)Y-Sb(2)S(3) and (99m)Tc-Sb(2)S(3) were found to have a diameter of 28.92 +/- 0.14 and 35.61 +/- 0.11 nm, respectively, by PCS. By TEM, (90)Y-Sb(2)S(3) particles were measured to be 14.33 +/- 0.09 nm. (90)Y-labelled Sn colloid were found to exist with a d(v(max1)) of 805 nm and a d(v(max2)) of 2590 nm, by PCS, whereas (99m)Tc-Sn colloid was shown to have more than 80% of radioactive particles of approximately 910 nm by PCS. For (90)Y-labelled Sb(2)S(3) and Sn colloid, a comparison of TEM and PCS indicates that these techniques found significantly different mean diameters. TEM has an excellent resolution necessary for radiocolloid particle-sizing analysis, and it is a desirable size-measuring technique because it is more reliable than PCS.
T2  - Journal of Microscopy, Oxford
T1  - Particle size analysis: (90)Y and (99m)Tc-labelled colloids
VL  - 232
IS  - 3
SP  - 601
EP  - 604
DO  - 10.1111/j.1365-2818.2008.02124.x
ER  - 

@article{
author = "Janković, Drina and Maksin, Tatjana N. and Đokić, Divna Đ. and Milonjić, Slobodan K. and Nikolić, Nadežda S. and Mirković, Marija D. and Vranješ-Đurić, Sanja",
year = "2008",
abstract = "Colloidal particle size is an important characteristic to consider when choosing a radiopharmaceutical for diagnosis and therapeutic purposes in nuclear medicine. Photon correlation spectroscopy (PCS) and transmission electron microscopy (TEM) were used to determine the particle-size distribution of (90)Y- and (99m)Tc-labelled antimony trisulfide (Sb(2)S(3)) and tin colloids (Sn-colloid). (90)Y-Sb(2)S(3) and (99m)Tc-Sb(2)S(3) were found to have a diameter of 28.92 +/- 0.14 and 35.61 +/- 0.11 nm, respectively, by PCS. By TEM, (90)Y-Sb(2)S(3) particles were measured to be 14.33 +/- 0.09 nm. (90)Y-labelled Sn colloid were found to exist with a d(v(max1)) of 805 nm and a d(v(max2)) of 2590 nm, by PCS, whereas (99m)Tc-Sn colloid was shown to have more than 80% of radioactive particles of approximately 910 nm by PCS. For (90)Y-labelled Sb(2)S(3) and Sn colloid, a comparison of TEM and PCS indicates that these techniques found significantly different mean diameters. TEM has an excellent resolution necessary for radiocolloid particle-sizing analysis, and it is a desirable size-measuring technique because it is more reliable than PCS.",
journal = "Journal of Microscopy, Oxford",
title = "Particle size analysis: (90)Y and (99m)Tc-labelled colloids",
volume = "232",
number = "3",
pages = "601-604",
doi = "10.1111/j.1365-2818.2008.02124.x"
}

Janković, D., Maksin, T. N., Đokić, D. Đ., Milonjić, S. K., Nikolić, N. S., Mirković, M. D.,& Vranješ-Đurić, S.. (2008). Particle size analysis: (90)Y and (99m)Tc-labelled colloids. in Journal of Microscopy, Oxford, 232(3), 601-604.
https://doi.org/10.1111/j.1365-2818.2008.02124.x

Janković D, Maksin TN, Đokić DĐ, Milonjić SK, Nikolić NS, Mirković MD, Vranješ-Đurić S. Particle size analysis: (90)Y and (99m)Tc-labelled colloids. in Journal of Microscopy, Oxford. 2008;232(3):601-604.
doi:10.1111/j.1365-2818.2008.02124.x .

Janković, Drina, Maksin, Tatjana N., Đokić, Divna Đ., Milonjić, Slobodan K., Nikolić, Nadežda S., Mirković, Marija D., Vranješ-Đurić, Sanja, "Particle size analysis: (90)Y and (99m)Tc-labelled colloids" in Journal of Microscopy, Oxford, 232, no. 3 (2008):601-604,
https://doi.org/10.1111/j.1365-2818.2008.02124.x . .