TY  - JOUR
AU  - Pavelkić, Vesna M.
AU  - Brdarić, Tanja
AU  - Petrović, Marija P.
AU  - Šekularac, Gavrilo M.
AU  - Košević, Milica G.
AU  - Pezo, Lato
AU  - Ilić Marija A. 
PY  - 2015
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/944
AB  - The applicability of Peleg model was investigated for predicting mass transfer kinetics during the osmotic dehydration (OD) process of pears, at different concentrations (40, 60 and 70%, w/w) and temperatures (20, 35 and 50 degrees C) of sucrose solution. Increase in sucrose solution concentration resulted in higher water loss (WL) and solid gain (SG) values through the osmotic treatment period. After 360 min of osmotic treatment of pears, WL ranged from 23.71 to 31.68% at 20 degrees C, from 24.80 to 40.38% at 35 degrees C and from 33.30 to 52.07% at 50 degrees C of initial weight of pears. The increase of dry mass of the samples, SG, after 360 min of osmotic treatment ranged from 3.02 to 6.68% at 20 degrees C, from 4.15 to 7.71% at 35 degrees C and from 5.00 to 8.92% at 50 degrees C. Pelegs rate constants, k(1)(WL) and k(1)(SG), decreased with increasing temperature, as well as decreased with increasing concentration of osmotic solution at constant temperature. Both capacity constants k(2)(WL) and k(2)(SG) also exhibited the inverse relationship between capacity constant and temperature, as well as concentration of the osmotic solution. Pelegs rate constants for WL and SG at all temperatures followed an Arrhenius type relationship. The predicted equilibrium values were very close to experimental ones, which was confirmed with high coefficients of determination and by the residual analysis.
T2  - Chemical Industry and Chemical Engineering Quarterly / CICEQ
T1  - Application of Peleg Model on Mass Transfer Kinetics During Osmotic Dehydratation of Pear Cubes in Sucrose Solution
VL  - 21
IS  - 4
SP  - 485
EP  - 492
DO  - 10.2298/CICEQ141014004P
ER  - 

@article{
author = "Pavelkić, Vesna M. and Brdarić, Tanja and Petrović, Marija P. and Šekularac, Gavrilo M. and Košević, Milica G. and Pezo, Lato and Ilić Marija A. ",
year = "2015",
abstract = "The applicability of Peleg model was investigated for predicting mass transfer kinetics during the osmotic dehydration (OD) process of pears, at different concentrations (40, 60 and 70%, w/w) and temperatures (20, 35 and 50 degrees C) of sucrose solution. Increase in sucrose solution concentration resulted in higher water loss (WL) and solid gain (SG) values through the osmotic treatment period. After 360 min of osmotic treatment of pears, WL ranged from 23.71 to 31.68% at 20 degrees C, from 24.80 to 40.38% at 35 degrees C and from 33.30 to 52.07% at 50 degrees C of initial weight of pears. The increase of dry mass of the samples, SG, after 360 min of osmotic treatment ranged from 3.02 to 6.68% at 20 degrees C, from 4.15 to 7.71% at 35 degrees C and from 5.00 to 8.92% at 50 degrees C. Pelegs rate constants, k(1)(WL) and k(1)(SG), decreased with increasing temperature, as well as decreased with increasing concentration of osmotic solution at constant temperature. Both capacity constants k(2)(WL) and k(2)(SG) also exhibited the inverse relationship between capacity constant and temperature, as well as concentration of the osmotic solution. Pelegs rate constants for WL and SG at all temperatures followed an Arrhenius type relationship. The predicted equilibrium values were very close to experimental ones, which was confirmed with high coefficients of determination and by the residual analysis.",
journal = "Chemical Industry and Chemical Engineering Quarterly / CICEQ",
title = "Application of Peleg Model on Mass Transfer Kinetics During Osmotic Dehydratation of Pear Cubes in Sucrose Solution",
volume = "21",
number = "4",
pages = "485-492",
doi = "10.2298/CICEQ141014004P"
}

Pavelkić, V. M., Brdarić, T., Petrović, M. P., Šekularac, G. M., Košević, M. G., Pezo, L.,& Ilić Marija A. . (2015). Application of Peleg Model on Mass Transfer Kinetics During Osmotic Dehydratation of Pear Cubes in Sucrose Solution. in Chemical Industry and Chemical Engineering Quarterly / CICEQ, 21(4), 485-492.
https://doi.org/10.2298/CICEQ141014004P

Pavelkić VM, Brdarić T, Petrović MP, Šekularac GM, Košević MG, Pezo L, Ilić Marija A. . Application of Peleg Model on Mass Transfer Kinetics During Osmotic Dehydratation of Pear Cubes in Sucrose Solution. in Chemical Industry and Chemical Engineering Quarterly / CICEQ. 2015;21(4):485-492.
doi:10.2298/CICEQ141014004P .

Pavelkić, Vesna M., Brdarić, Tanja, Petrović, Marija P., Šekularac, Gavrilo M., Košević, Milica G., Pezo, Lato, Ilić Marija A. , "Application of Peleg Model on Mass Transfer Kinetics During Osmotic Dehydratation of Pear Cubes in Sucrose Solution" in Chemical Industry and Chemical Engineering Quarterly / CICEQ, 21, no. 4 (2015):485-492,
https://doi.org/10.2298/CICEQ141014004P . .

TY  - JOUR
AU  - Rastegari, Ali Asghar
AU  - Buzari, Behnaz
AU  - Pavelkić, Vesna M.
AU  - Gopčević, Kristina
AU  - Petković, Marijana
AU  - Bordbar, Abdol-Khalegh
PY  - 2013
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/5664
AB  - The thermal stability of pepsin in a strong acid medium as a function of pH has been investigated using differential scanning calorimetry (DSC), UV absorbance, polyacrylamide gel electrophoresis (PAGE) and MALDI-TOF MS methods. The two independent two-state transitions model with view of physiological function of pepsin was used for analyzing thermal denaturation curves. The transition temperature (T-m) values ranging from 305.15 to 319.15K for the first transition and from 322.15 to 349.15K for the second transition in the examined pH range implicating the higher stability at pH 4 are in good agreement with MALDI-TOF MS results. The corresponding maximum, Delta G degrees(25), was stability obtained at pH 4 with values of 65.3 kJ mol(-1). (C) 2013 Elsevier B.V. All rights reserved.
T2  - Thermochimica Acta
T1  - Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques
VL  - 568
SP  - 165
EP  - 170
DO  - 10.1016/j.tca.2013.06.030
ER  - 

@article{
author = "Rastegari, Ali Asghar and Buzari, Behnaz and Pavelkić, Vesna M. and Gopčević, Kristina and Petković, Marijana and Bordbar, Abdol-Khalegh",
year = "2013",
abstract = "The thermal stability of pepsin in a strong acid medium as a function of pH has been investigated using differential scanning calorimetry (DSC), UV absorbance, polyacrylamide gel electrophoresis (PAGE) and MALDI-TOF MS methods. The two independent two-state transitions model with view of physiological function of pepsin was used for analyzing thermal denaturation curves. The transition temperature (T-m) values ranging from 305.15 to 319.15K for the first transition and from 322.15 to 349.15K for the second transition in the examined pH range implicating the higher stability at pH 4 are in good agreement with MALDI-TOF MS results. The corresponding maximum, Delta G degrees(25), was stability obtained at pH 4 with values of 65.3 kJ mol(-1). (C) 2013 Elsevier B.V. All rights reserved.",
journal = "Thermochimica Acta",
title = "Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques",
volume = "568",
pages = "165-170",
doi = "10.1016/j.tca.2013.06.030"
}

Rastegari, A. A., Buzari, B., Pavelkić, V. M., Gopčević, K., Petković, M.,& Bordbar, A.. (2013). Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques. in Thermochimica Acta, 568, 165-170.
https://doi.org/10.1016/j.tca.2013.06.030

Rastegari AA, Buzari B, Pavelkić VM, Gopčević K, Petković M, Bordbar A. Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques. in Thermochimica Acta. 2013;568:165-170.
doi:10.1016/j.tca.2013.06.030 .

Rastegari, Ali Asghar, Buzari, Behnaz, Pavelkić, Vesna M., Gopčević, Kristina, Petković, Marijana, Bordbar, Abdol-Khalegh, "Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques" in Thermochimica Acta, 568 (2013):165-170,
https://doi.org/10.1016/j.tca.2013.06.030 . .

TY  - CONF
AU  - Pavelkić, Vesna M.
AU  - Antić, K.
AU  - Babić, M.
AU  - Gopčević, Kristina
AU  - Petković, Marijana
PY  - 2012
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9301
AB  - To obtain detailed information about properties of pepsin in thermal denaturing
conditions, polyacrylamide gel electrophoresis (PAGE) and matrix-assisted laser
desorption-ionization time-of-flight mass spectrometry (MALDI-TOF MS)
experimental data were analyzed. These methods were used to analyze the changes
in the structural properties of pepsin molecule subjected to broad-range
temperature variations, from 25 ºC to 70 ºC, and pH range from 1 to 4.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2012 : 11th international conference on fundamental and applied aspects of physical chemistry
T1  - Analysis of thermal denaturation of pepsin on basis of MALDI-TOF MS and PAGE experimental data
VL  - 1
SP  - 397
EP  - 399
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9301
ER  - 

@conference{
author = "Pavelkić, Vesna M. and Antić, K. and Babić, M. and Gopčević, Kristina and Petković, Marijana",
year = "2012",
abstract = "To obtain detailed information about properties of pepsin in thermal denaturing
conditions, polyacrylamide gel electrophoresis (PAGE) and matrix-assisted laser
desorption-ionization time-of-flight mass spectrometry (MALDI-TOF MS)
experimental data were analyzed. These methods were used to analyze the changes
in the structural properties of pepsin molecule subjected to broad-range
temperature variations, from 25 ºC to 70 ºC, and pH range from 1 to 4.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2012 : 11th international conference on fundamental and applied aspects of physical chemistry",
title = "Analysis of thermal denaturation of pepsin on basis of MALDI-TOF MS and PAGE experimental data",
volume = "1",
pages = "397-399",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9301"
}

Pavelkić, V. M., Antić, K., Babić, M., Gopčević, K.,& Petković, M.. (2012). Analysis of thermal denaturation of pepsin on basis of MALDI-TOF MS and PAGE experimental data. in Physical chemistry 2012 : 11th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia., 1, 397-399.
https://hdl.handle.net/21.15107/rcub_vinar_9301

Pavelkić VM, Antić K, Babić M, Gopčević K, Petković M. Analysis of thermal denaturation of pepsin on basis of MALDI-TOF MS and PAGE experimental data. in Physical chemistry 2012 : 11th international conference on fundamental and applied aspects of physical chemistry. 2012;1:397-399.
https://hdl.handle.net/21.15107/rcub_vinar_9301 .

Pavelkić, Vesna M., Antić, K., Babić, M., Gopčević, Kristina, Petković, Marijana, "Analysis of thermal denaturation of pepsin on basis of MALDI-TOF MS and PAGE experimental data" in Physical chemistry 2012 : 11th international conference on fundamental and applied aspects of physical chemistry, 1 (2012):397-399,
https://hdl.handle.net/21.15107/rcub_vinar_9301 .

TY  - CONF
AU  - Pavelkić, Vesna M.
AU  - Gopčević, Kristina
AU  - Krstić, Danijela Z.
AU  - Ilić, Milan
AU  - Pavelkić, M.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9371
AB  - The in vitro effect of Al3+ ions on pepsin activity at pH 2, via kinetic parameters was evaluated. Kinetic study showed that Al3+ ions increase the maximal velocity (Vmax) rather than apparent affinity for substrate (KS) implying the non-competitive nature of activation which indicated that aluminium was a non-essential activator of partial non-competitive type.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
T1  - Non-essential activation of pepsin by Al3+ “in vitro”
VL  - 1
SP  - 393
EP  - 395
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9371
ER  - 

@conference{
author = "Pavelkić, Vesna M. and Gopčević, Kristina and Krstić, Danijela Z. and Ilić, Milan and Pavelkić, M.",
year = "2008",
abstract = "The in vitro effect of Al3+ ions on pepsin activity at pH 2, via kinetic parameters was evaluated. Kinetic study showed that Al3+ ions increase the maximal velocity (Vmax) rather than apparent affinity for substrate (KS) implying the non-competitive nature of activation which indicated that aluminium was a non-essential activator of partial non-competitive type.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry",
title = "Non-essential activation of pepsin by Al3+ “in vitro”",
volume = "1",
pages = "393-395",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9371"
}

Pavelkić, V. M., Gopčević, K., Krstić, D. Z., Ilić, M.,& Pavelkić, M.. (2008). Non-essential activation of pepsin by Al3+ “in vitro”. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia., 1, 393-395.
https://hdl.handle.net/21.15107/rcub_vinar_9371

Pavelkić VM, Gopčević K, Krstić DZ, Ilić M, Pavelkić M. Non-essential activation of pepsin by Al3+ “in vitro”. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry. 2008;1:393-395.
https://hdl.handle.net/21.15107/rcub_vinar_9371 .

Pavelkić, Vesna M., Gopčević, Kristina, Krstić, Danijela Z., Ilić, Milan, Pavelkić, M., "Non-essential activation of pepsin by Al3+ “in vitro”" in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry, 1 (2008):393-395,
https://hdl.handle.net/21.15107/rcub_vinar_9371 .

TY  - JOUR
AU  - Pavelkić, Vesna M.
AU  - Gopčević, Kristina
AU  - Krstić, Danijela Z.
AU  - Ilić Marija A. 
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3566
AB  - The in vitro effect of Al3+ ions in the concentration range 1.710-6M-8.710-3M on pepsin activity at pH 2, via kinetic parameters and its electrophoretic mobility was evaluated. Kinetic study demonstrated the existence of an activation effect of Al3+ at pH 2 on pepsin molecule. Kinetic analysis with respect to concentrations of haemoglobin showed that Al3+ ions increase the maximal velocity (Vmax) and kcat values rather than apparent affinity for substrate (KS) implying the non-competitive nature of activation which indicated that aluminium was a non-essential activator of partial non-competitive type. The values of the equilibrium constants KS and KmA for dissociation of corresponding complexes were evaluated as 0.9040.083mM and 8.560.51M, respectively. Dissociation constant KA, of activator from enzyme-activator complex calculated via kinetic and direct measurement of Al3+ binding data, as well as activation constant A50, the activator concentration that gives a rate equal to half at a saturating concentration of activator, were found to be 8.820.90M, 8.390.76M, and 8.050.48M respectively. Native PAGE electrophoresis shows the decrease in electrophoretic mobility of pepsin and confirms modification of the electric charge and conformational changes of pepsin caused by bound Al3+ on the pepsin molecule. Al3+ induced conformational changes of pepsin were verified by UV-VIS and IR spectra. Moreover, the absence of conformational changes in the haemoglobin molecule in the presence of Al3+ ions confirms that the obtained activation is a consequence of conformational changes caused only in the pepsin molecule.
T2  - Journal of Enzyme Inhibition and Medicinal Chemistry
T1  - The influence of Al3+ion on porcine pepsin activity in vitro
VL  - 23
IS  - 6
SP  - 1002
EP  - 1010
DO  - 10.1080/14756360701841095
ER  - 

@article{
author = "Pavelkić, Vesna M. and Gopčević, Kristina and Krstić, Danijela Z. and Ilić Marija A. ",
year = "2008",
abstract = "The in vitro effect of Al3+ ions in the concentration range 1.710-6M-8.710-3M on pepsin activity at pH 2, via kinetic parameters and its electrophoretic mobility was evaluated. Kinetic study demonstrated the existence of an activation effect of Al3+ at pH 2 on pepsin molecule. Kinetic analysis with respect to concentrations of haemoglobin showed that Al3+ ions increase the maximal velocity (Vmax) and kcat values rather than apparent affinity for substrate (KS) implying the non-competitive nature of activation which indicated that aluminium was a non-essential activator of partial non-competitive type. The values of the equilibrium constants KS and KmA for dissociation of corresponding complexes were evaluated as 0.9040.083mM and 8.560.51M, respectively. Dissociation constant KA, of activator from enzyme-activator complex calculated via kinetic and direct measurement of Al3+ binding data, as well as activation constant A50, the activator concentration that gives a rate equal to half at a saturating concentration of activator, were found to be 8.820.90M, 8.390.76M, and 8.050.48M respectively. Native PAGE electrophoresis shows the decrease in electrophoretic mobility of pepsin and confirms modification of the electric charge and conformational changes of pepsin caused by bound Al3+ on the pepsin molecule. Al3+ induced conformational changes of pepsin were verified by UV-VIS and IR spectra. Moreover, the absence of conformational changes in the haemoglobin molecule in the presence of Al3+ ions confirms that the obtained activation is a consequence of conformational changes caused only in the pepsin molecule.",
journal = "Journal of Enzyme Inhibition and Medicinal Chemistry",
title = "The influence of Al3+ion on porcine pepsin activity in vitro",
volume = "23",
number = "6",
pages = "1002-1010",
doi = "10.1080/14756360701841095"
}

Pavelkić, V. M., Gopčević, K., Krstić, D. Z.,& Ilić Marija A. . (2008). The influence of Al3+ion on porcine pepsin activity in vitro. in Journal of Enzyme Inhibition and Medicinal Chemistry, 23(6), 1002-1010.
https://doi.org/10.1080/14756360701841095

Pavelkić VM, Gopčević K, Krstić DZ, Ilić Marija A. . The influence of Al3+ion on porcine pepsin activity in vitro. in Journal of Enzyme Inhibition and Medicinal Chemistry. 2008;23(6):1002-1010.
doi:10.1080/14756360701841095 .

Pavelkić, Vesna M., Gopčević, Kristina, Krstić, Danijela Z., Ilić Marija A. , "The influence of Al3+ion on porcine pepsin activity in vitro" in Journal of Enzyme Inhibition and Medicinal Chemistry, 23, no. 6 (2008):1002-1010,
https://doi.org/10.1080/14756360701841095 . .

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  - CONF
AU  - Stanisavljev, Dragomir R.
AU  - Pavelkić, Vesna M.
AU  - Beljanski, Vladimir
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9373
AB  - Kinetic study of microwave (MW) irradiated enzyme pepsin was performed. Decreased enzyme activity was observed, under constant temperature and absorbed MW energy per time unit. In accordance with experimental conditions, Vmax and Km were calculated for irradiated pepsin solutions and compared with control reaction with non-irradiated pepsin.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
T1  - Microwawe irradiation influence on enzyme kinetics
VL  - 1
SP  - 405
EP  - 407
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9373
ER  - 

@conference{
author = "Stanisavljev, Dragomir R. and Pavelkić, Vesna M. and Beljanski, Vladimir",
year = "2008",
abstract = "Kinetic study of microwave (MW) irradiated enzyme pepsin was performed. Decreased enzyme activity was observed, under constant temperature and absorbed MW energy per time unit. In accordance with experimental conditions, Vmax and Km were calculated for irradiated pepsin solutions and compared with control reaction with non-irradiated pepsin.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry",
title = "Microwawe irradiation influence on enzyme kinetics",
volume = "1",
pages = "405-407",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9373"
}

Stanisavljev, D. R., Pavelkić, V. M.,& Beljanski, V.. (2008). Microwawe irradiation influence on enzyme kinetics. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia., 1, 405-407.
https://hdl.handle.net/21.15107/rcub_vinar_9373

Stanisavljev DR, Pavelkić VM, Beljanski V. Microwawe irradiation influence on enzyme kinetics. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry. 2008;1:405-407.
https://hdl.handle.net/21.15107/rcub_vinar_9373 .

Stanisavljev, Dragomir R., Pavelkić, Vesna M., Beljanski, Vladimir, "Microwawe irradiation influence on enzyme kinetics" in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry, 1 (2008):405-407,
https://hdl.handle.net/21.15107/rcub_vinar_9373 .

TY  - CONF
AU  - Pavelkić, Vesna M.
AU  - Stanisavljev, Dragomir R.
AU  - Gopčević, Kristina
AU  - Beljanski, Vladimir
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9358
AB  - Microwave (MW) irradiated bovine serum albumin (BSA) and bromphenol blue (BPB) complex was used as substrate for the assay of pepsin by kinetic method. Decreased reaction velocity under absorbed MW energy and constant temperature was observed.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
T1  - Effects of microwave treated substrate on pepsin reaction kinetics
VL  - 1
SP  - 166
EP  - 168
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9358
ER  - 

@conference{
author = "Pavelkić, Vesna M. and Stanisavljev, Dragomir R. and Gopčević, Kristina and Beljanski, Vladimir",
year = "2008",
abstract = "Microwave (MW) irradiated bovine serum albumin (BSA) and bromphenol blue (BPB) complex was used as substrate for the assay of pepsin by kinetic method. Decreased reaction velocity under absorbed MW energy and constant temperature was observed.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry",
title = "Effects of microwave treated substrate on pepsin reaction kinetics",
volume = "1",
pages = "166-168",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9358"
}

Pavelkić, V. M., Stanisavljev, D. R., Gopčević, K.,& Beljanski, V.. (2008). Effects of microwave treated substrate on pepsin reaction kinetics. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia., 1, 166-168.
https://hdl.handle.net/21.15107/rcub_vinar_9358

Pavelkić VM, Stanisavljev DR, Gopčević K, Beljanski V. Effects of microwave treated substrate on pepsin reaction kinetics. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry. 2008;1:166-168.
https://hdl.handle.net/21.15107/rcub_vinar_9358 .

Pavelkić, Vesna M., Stanisavljev, Dragomir R., Gopčević, Kristina, Beljanski, Vladimir, "Effects of microwave treated substrate on pepsin reaction kinetics" in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry, 1 (2008):166-168,
https://hdl.handle.net/21.15107/rcub_vinar_9358 .

TY  - CONF
AU  - Pavelkić, Vesna M.
AU  - Gopčević, Kristina
AU  - Krstić, Danijela Z.
AU  - Ilić, Milan
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9426
AB  - The influence of temperature and different concentrations of Al3+ on pepsin electrophoretic mobility was investigated. The increase of Al3+ concentrations causes the decrease the electrophoretic mobility of enzyme. Also the increase of temperature induced the same effect. The influence of both temperature and Al3+ ion concentrations is additive.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry
T1  - Temperature and Al3+ influence on electrophoretic mobility of porcine pepsin
SP  - 374
EP  - 376
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9426
ER  - 

@conference{
author = "Pavelkić, Vesna M. and Gopčević, Kristina and Krstić, Danijela Z. and Ilić, Milan",
year = "2006",
abstract = "The influence of temperature and different concentrations of Al3+ on pepsin electrophoretic mobility was investigated. The increase of Al3+ concentrations causes the decrease the electrophoretic mobility of enzyme. Also the increase of temperature induced the same effect. The influence of both temperature and Al3+ ion concentrations is additive.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry",
title = "Temperature and Al3+ influence on electrophoretic mobility of porcine pepsin",
pages = "374-376",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9426"
}

Pavelkić, V. M., Gopčević, K., Krstić, D. Z.,& Ilić, M.. (2006). Temperature and Al3+ influence on electrophoretic mobility of porcine pepsin. in Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry
Society of Physical Chemists of Serbia., 374-376.
https://hdl.handle.net/21.15107/rcub_vinar_9426

Pavelkić VM, Gopčević K, Krstić DZ, Ilić M. Temperature and Al3+ influence on electrophoretic mobility of porcine pepsin. in Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry. 2006;:374-376.
https://hdl.handle.net/21.15107/rcub_vinar_9426 .

Pavelkić, Vesna M., Gopčević, Kristina, Krstić, Danijela Z., Ilić, Milan, "Temperature and Al3+ influence on electrophoretic mobility of porcine pepsin" in Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry (2006):374-376,
https://hdl.handle.net/21.15107/rcub_vinar_9426 .

TY  - JOUR
AU  - Vasić, Vesna M.
AU  - Savić, Jasmina
AU  - Pavelkić, Vesna M.
AU  - Milonjić, Slobodan K.
PY  - 2005
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2944
T2  - Colloids and Surfaces. A: Physicochemical and Engineering Aspects
T1  - Erratum: Kinetics of 1,8-dihydroxy-2-(pyrazol-5-ylazo)-naphthalene-3,6-disulphonic acid immobilization on anion exchangers (vol 215, pg 277, 2003)
VL  - 268
IS  - 1-3
SP  - 180
EP  - 180
DO  - 10.1016/j.colsurfa.2005.08.001
ER  - 

@article{
author = "Vasić, Vesna M. and Savić, Jasmina and Pavelkić, Vesna M. and Milonjić, Slobodan K.",
year = "2005",
journal = "Colloids and Surfaces. A: Physicochemical and Engineering Aspects",
title = "Erratum: Kinetics of 1,8-dihydroxy-2-(pyrazol-5-ylazo)-naphthalene-3,6-disulphonic acid immobilization on anion exchangers (vol 215, pg 277, 2003)",
volume = "268",
number = "1-3",
pages = "180-180",
doi = "10.1016/j.colsurfa.2005.08.001"
}

Vasić, V. M., Savić, J., Pavelkić, V. M.,& Milonjić, S. K.. (2005). Erratum: Kinetics of 1,8-dihydroxy-2-(pyrazol-5-ylazo)-naphthalene-3,6-disulphonic acid immobilization on anion exchangers (vol 215, pg 277, 2003). in Colloids and Surfaces. A: Physicochemical and Engineering Aspects, 268(1-3), 180-180.
https://doi.org/10.1016/j.colsurfa.2005.08.001

Vasić VM, Savić J, Pavelkić VM, Milonjić SK. Erratum: Kinetics of 1,8-dihydroxy-2-(pyrazol-5-ylazo)-naphthalene-3,6-disulphonic acid immobilization on anion exchangers (vol 215, pg 277, 2003). in Colloids and Surfaces. A: Physicochemical and Engineering Aspects. 2005;268(1-3):180-180.
doi:10.1016/j.colsurfa.2005.08.001 .

Vasić, Vesna M., Savić, Jasmina, Pavelkić, Vesna M., Milonjić, Slobodan K., "Erratum: Kinetics of 1,8-dihydroxy-2-(pyrazol-5-ylazo)-naphthalene-3,6-disulphonic acid immobilization on anion exchangers (vol 215, pg 277, 2003)" in Colloids and Surfaces. A: Physicochemical and Engineering Aspects, 268, no. 1-3 (2005):180-180,
https://doi.org/10.1016/j.colsurfa.2005.08.001 . .

TY  - JOUR
AU  - Đurđević, Predrag
AU  - Cvijović, Mirjana R.
AU  - Pavelkić, Vesna M.
AU  - Zakrzewska, J
PY  - 2005
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2967
AB  - The complex formation between L-histidine (HHis) and aluminum(III) ion in water solutions was studied by UV spectrophotometric and 27-Al NMR measurements at 298 K. UV spectra were measured on solutions in which the total concentration of histidine was from 15.0 to 50.0 mmol/dm(3) and the concentration ratio of histidine to aluminum was varied from 3 : 1 to 10 : 1 in the pH range between 4.2 and 6.0. The spectra were taken in the wavelength interval 240 - 340 nm. Nonlinear least-squares treatment of the spectrophotometric data indicates the formation of the complexes Al(HHis)(3+), Al(His)(2+), Al(HHis)His(2+), and Al-2(OH)His(4+) with the overall formation constants beta(p,q,r): log beta(1,1,1) = 11.90 +/- 0.04, log beta(1,1,0) = 7.25 +/- 0.08, log beta(1,2,1) = 20.1 +/- 0.1, and log beta(2,1,1) = 5.92 +/- 0.12 ( p, q, r are stoichiometric indices for metal, ligand, and proton, respectively). Al-27-NMR spectra were taken on solutions with the concentration of aluminum 50 mmol/dm(3) and that of histidine 250 mmol/dm(3). In the pH interval 5.0 - 6.1, two resonances at 9.5 ppm and 12.0 ppm were assigned to Al(HHis)(2+) and Al( HHis)(His)(2+) (or Al(OH)(HHis)(2)(2+)), respectively.
T2  - Spectroscopy Letters
T1  - Spectrophotometric and 27-Al NMR characterization of aluminum(III) complexes with L-histidine
VL  - 38
IS  - 4-5
SP  - 617
EP  - 634
DO  - 10.1081/SL-200062968
ER  - 

@article{
author = "Đurđević, Predrag and Cvijović, Mirjana R. and Pavelkić, Vesna M. and Zakrzewska, J",
year = "2005",
abstract = "The complex formation between L-histidine (HHis) and aluminum(III) ion in water solutions was studied by UV spectrophotometric and 27-Al NMR measurements at 298 K. UV spectra were measured on solutions in which the total concentration of histidine was from 15.0 to 50.0 mmol/dm(3) and the concentration ratio of histidine to aluminum was varied from 3 : 1 to 10 : 1 in the pH range between 4.2 and 6.0. The spectra were taken in the wavelength interval 240 - 340 nm. Nonlinear least-squares treatment of the spectrophotometric data indicates the formation of the complexes Al(HHis)(3+), Al(His)(2+), Al(HHis)His(2+), and Al-2(OH)His(4+) with the overall formation constants beta(p,q,r): log beta(1,1,1) = 11.90 +/- 0.04, log beta(1,1,0) = 7.25 +/- 0.08, log beta(1,2,1) = 20.1 +/- 0.1, and log beta(2,1,1) = 5.92 +/- 0.12 ( p, q, r are stoichiometric indices for metal, ligand, and proton, respectively). Al-27-NMR spectra were taken on solutions with the concentration of aluminum 50 mmol/dm(3) and that of histidine 250 mmol/dm(3). In the pH interval 5.0 - 6.1, two resonances at 9.5 ppm and 12.0 ppm were assigned to Al(HHis)(2+) and Al( HHis)(His)(2+) (or Al(OH)(HHis)(2)(2+)), respectively.",
journal = "Spectroscopy Letters",
title = "Spectrophotometric and 27-Al NMR characterization of aluminum(III) complexes with L-histidine",
volume = "38",
number = "4-5",
pages = "617-634",
doi = "10.1081/SL-200062968"
}

Đurđević, P., Cvijović, M. R., Pavelkić, V. M.,& Zakrzewska, J.. (2005). Spectrophotometric and 27-Al NMR characterization of aluminum(III) complexes with L-histidine. in Spectroscopy Letters, 38(4-5), 617-634.
https://doi.org/10.1081/SL-200062968

Đurđević P, Cvijović MR, Pavelkić VM, Zakrzewska J. Spectrophotometric and 27-Al NMR characterization of aluminum(III) complexes with L-histidine. in Spectroscopy Letters. 2005;38(4-5):617-634.
doi:10.1081/SL-200062968 .

Đurđević, Predrag, Cvijović, Mirjana R., Pavelkić, Vesna M., Zakrzewska, J, "Spectrophotometric and 27-Al NMR characterization of aluminum(III) complexes with L-histidine" in Spectroscopy Letters, 38, no. 4-5 (2005):617-634,
https://doi.org/10.1081/SL-200062968 . .

TY  - CONF
AU  - Pavelkić, Vesna M.
AU  - Živanović, Miloš Z.
AU  - Spasojević-Tišma, Vera D.
AU  - Ilić, Milan
PY  - 2004
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9490
AB  - Heat aggregation of pepsin, in a strong acid media; involve the stage of nucleation, and the stage of growth of aggregates. The initial parts of the kinetic curves of aggregation were followed via monitoring the increase of absorbance (A) and were linearized as {dA/dt; t} and {A; t 2 } functions. The slope of these curves is proportional to the product rate constant of reversible denaturation and the rate constant of growth of aggregates. Addition of Al3+ ions display a lag period whose appearance is caused by intramolecular predenaturational changes in the pepsin molecule.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry
T1  - Kinetics of heat denaturation of pepsin in a strong acid media
VL  - 1
SP  - 240
EP  - 242
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9490
ER  - 

@conference{
author = "Pavelkić, Vesna M. and Živanović, Miloš Z. and Spasojević-Tišma, Vera D. and Ilić, Milan",
year = "2004",
abstract = "Heat aggregation of pepsin, in a strong acid media; involve the stage of nucleation, and the stage of growth of aggregates. The initial parts of the kinetic curves of aggregation were followed via monitoring the increase of absorbance (A) and were linearized as {dA/dt; t} and {A; t 2 } functions. The slope of these curves is proportional to the product rate constant of reversible denaturation and the rate constant of growth of aggregates. Addition of Al3+ ions display a lag period whose appearance is caused by intramolecular predenaturational changes in the pepsin molecule.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry",
title = "Kinetics of heat denaturation of pepsin in a strong acid media",
volume = "1",
pages = "240-242",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9490"
}

Pavelkić, V. M., Živanović, M. Z., Spasojević-Tišma, V. D.,& Ilić, M.. (2004). Kinetics of heat denaturation of pepsin in a strong acid media. in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry
Society of Physical Chemists of Serbia., 1, 240-242.
https://hdl.handle.net/21.15107/rcub_vinar_9490

Pavelkić VM, Živanović MZ, Spasojević-Tišma VD, Ilić M. Kinetics of heat denaturation of pepsin in a strong acid media. in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry. 2004;1:240-242.
https://hdl.handle.net/21.15107/rcub_vinar_9490 .

Pavelkić, Vesna M., Živanović, Miloš Z., Spasojević-Tišma, Vera D., Ilić, Milan, "Kinetics of heat denaturation of pepsin in a strong acid media" in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry, 1 (2004):240-242,
https://hdl.handle.net/21.15107/rcub_vinar_9490 .

TY  - CONF
AU  - Cvijović, Mirjana R.
AU  - Pavelkić, Vesna M.
AU  - Miljević, Nada R.
AU  - Stanisavljev, Dragomir R.
AU  - Đurđević, Predrag
PY  - 2004
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9602
AB  - Aluminium(III) ion and L-histidine (HHis) react in water solution to yield two mononuclear binary complexes [Al(HHis)]3+ and [Al(HHis)His] 2+. The over-all stability constants for these complexes were calculated by non-linearleast-squarestreatment of the spectrophotometric data and found to be: log β1,1,1 = 13.12 ± 0.04, log β1,2,1 = 20.9 ± 0.1, respectively. Indices refer to stoichiometric coefficients in complexation equilibrium: p Al + q His + r H → [AlpHisqHr]. The possible structures of the complexes in solution, are discussed.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry
T1  - Spectrophotometric study of solution equilibria between Al3+ ion and L-histidine
VL  - 2
SP  - 805
EP  - 807
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9602
ER  - 

@conference{
author = "Cvijović, Mirjana R. and Pavelkić, Vesna M. and Miljević, Nada R. and Stanisavljev, Dragomir R. and Đurđević, Predrag",
year = "2004",
abstract = "Aluminium(III) ion and L-histidine (HHis) react in water solution to yield two mononuclear binary complexes [Al(HHis)]3+ and [Al(HHis)His] 2+. The over-all stability constants for these complexes were calculated by non-linearleast-squarestreatment of the spectrophotometric data and found to be: log β1,1,1 = 13.12 ± 0.04, log β1,2,1 = 20.9 ± 0.1, respectively. Indices refer to stoichiometric coefficients in complexation equilibrium: p Al + q His + r H → [AlpHisqHr]. The possible structures of the complexes in solution, are discussed.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry",
title = "Spectrophotometric study of solution equilibria between Al3+ ion and L-histidine",
volume = "2",
pages = "805-807",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9602"
}

Cvijović, M. R., Pavelkić, V. M., Miljević, N. R., Stanisavljev, D. R.,& Đurđević, P.. (2004). Spectrophotometric study of solution equilibria between Al3+ ion and L-histidine. in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry
Society of Physical Chemists of Serbia., 2, 805-807.
https://hdl.handle.net/21.15107/rcub_vinar_9602

Cvijović MR, Pavelkić VM, Miljević NR, Stanisavljev DR, Đurđević P. Spectrophotometric study of solution equilibria between Al3+ ion and L-histidine. in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry. 2004;2:805-807.
https://hdl.handle.net/21.15107/rcub_vinar_9602 .

Cvijović, Mirjana R., Pavelkić, Vesna M., Miljević, Nada R., Stanisavljev, Dragomir R., Đurđević, Predrag, "Spectrophotometric study of solution equilibria between Al3+ ion and L-histidine" in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry, 2 (2004):805-807,
https://hdl.handle.net/21.15107/rcub_vinar_9602 .

TY  - JOUR
AU  - Vasić, Vesna M.
AU  - Savić, Jasmina
AU  - Pavelkić, Vesna M.
AU  - Milonjić, Slobodan K.
PY  - 2003
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2615
AB  - dThe sorption of 1,8-dihydroxy-2-(pyrazol-5-ylazo)-naphthalene-3,6-disulphonic acid (PACA) onto the anion exchange resins, Dowex 1-X8 and Dowex 2-X8, from aqueous solutions with pH between 1 and 10 was studied spectrophotometrically. Conditions for obtaining modified sorbents with a given capacity for the azo compound were determined. The absorption and reflectance spectra of the sorbed dye were recorded. The immobilized reagent retained similar chromic characteristics as in the solution. The sorption mechanism was investigated under static conditions in the temperature range from 0 to 25 degreesC, by determining the amount of sorbed dye as a function of contact time. The sorption was a first order process in all cases. The pore diffusion was found to be a rate-limiting step in the sorption process. The diffusion coefficient values from 6.0 to 7.4 x 10(-7) cm(2) s(-1) were calculated from the experimental results. The activation energy of PACA sorption is - 8.56 and - 8.05 kJ mol(-1) for Dowex 1-X8 and Dowex 2-X8, respectively. (C) 2002 Elsevier Science B.V. All rights reserved.
T2  - Colloids and Surfaces. A: Physicochemical and Engineering Aspects
T1  - Kinetics of 1,8-dihydroxy-2-(pyrazol-5-ylazo)-naphthalene-3,6-disulphonic acid immobilization on anion exchangers
VL  - 215
IS  - 1-3
SP  - 277
EP  - 284
DO  - 10.1016/S0927-7757(02)00490-9
ER  - 

@article{
author = "Vasić, Vesna M. and Savić, Jasmina and Pavelkić, Vesna M. and Milonjić, Slobodan K.",
year = "2003",
abstract = "dThe sorption of 1,8-dihydroxy-2-(pyrazol-5-ylazo)-naphthalene-3,6-disulphonic acid (PACA) onto the anion exchange resins, Dowex 1-X8 and Dowex 2-X8, from aqueous solutions with pH between 1 and 10 was studied spectrophotometrically. Conditions for obtaining modified sorbents with a given capacity for the azo compound were determined. The absorption and reflectance spectra of the sorbed dye were recorded. The immobilized reagent retained similar chromic characteristics as in the solution. The sorption mechanism was investigated under static conditions in the temperature range from 0 to 25 degreesC, by determining the amount of sorbed dye as a function of contact time. The sorption was a first order process in all cases. The pore diffusion was found to be a rate-limiting step in the sorption process. The diffusion coefficient values from 6.0 to 7.4 x 10(-7) cm(2) s(-1) were calculated from the experimental results. The activation energy of PACA sorption is - 8.56 and - 8.05 kJ mol(-1) for Dowex 1-X8 and Dowex 2-X8, respectively. (C) 2002 Elsevier Science B.V. All rights reserved.",
journal = "Colloids and Surfaces. A: Physicochemical and Engineering Aspects",
title = "Kinetics of 1,8-dihydroxy-2-(pyrazol-5-ylazo)-naphthalene-3,6-disulphonic acid immobilization on anion exchangers",
volume = "215",
number = "1-3",
pages = "277-284",
doi = "10.1016/S0927-7757(02)00490-9"
}

Vasić, V. M., Savić, J., Pavelkić, V. M.,& Milonjić, S. K.. (2003). Kinetics of 1,8-dihydroxy-2-(pyrazol-5-ylazo)-naphthalene-3,6-disulphonic acid immobilization on anion exchangers. in Colloids and Surfaces. A: Physicochemical and Engineering Aspects, 215(1-3), 277-284.
https://doi.org/10.1016/S0927-7757(02)00490-9

Vasić VM, Savić J, Pavelkić VM, Milonjić SK. Kinetics of 1,8-dihydroxy-2-(pyrazol-5-ylazo)-naphthalene-3,6-disulphonic acid immobilization on anion exchangers. in Colloids and Surfaces. A: Physicochemical and Engineering Aspects. 2003;215(1-3):277-284.
doi:10.1016/S0927-7757(02)00490-9 .

Vasić, Vesna M., Savić, Jasmina, Pavelkić, Vesna M., Milonjić, Slobodan K., "Kinetics of 1,8-dihydroxy-2-(pyrazol-5-ylazo)-naphthalene-3,6-disulphonic acid immobilization on anion exchangers" in Colloids and Surfaces. A: Physicochemical and Engineering Aspects, 215, no. 1-3 (2003):277-284,
https://doi.org/10.1016/S0927-7757(02)00490-9 . .

TY  - JOUR
AU  - Pavlović, Mirjana S.
AU  - Kuzmanović, Miroslav M.
AU  - Pavelkić, Vesna M.
AU  - Marinković, Miloš
PY  - 2000
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2372
AB  - The effect of easily ionized elements (EIE) in d.c. plasma (DCP) has been modeled and experimentally investigated. The introduction of the EIEs in the U-shaped DCP decreases a potential barrier due to an internal radial electric field, which allows the partially ionized analyte better entry into the hot plasma zone and produces enhancement of the analyte spectral emission. Compared to the equilibrium concentration, the increased electron concentration in the fringe region due to large radial gradients is accounted for in the model. By comparing model predictions to experimental data, the validity of the model is tested. The main features of the effect, the large enhancement at small addition of EIE and almost equal enhancement of ion and atom line intensities, are fairly well described by the model. The results are believed to be applicable to the inverted Y-shaped DCP. The effect in the inductively coupled plasma (ICP) has been briefly discussed from the point of view of the proposed model. (C) 2000 Elsevier Science B.V. All rights reserved.
T2  - Spectrochimica Acta. Part B: Atomic Spectroscopy
T1  - The role of demixing effect in analyte emission enhancement by easily ionized elements in d.c. plasma
VL  - 55
IS  - 8
SP  - 1373
EP  - 1384
DO  - 10.1016/S0584-8547(00)00242-1
ER  - 

@article{
author = "Pavlović, Mirjana S. and Kuzmanović, Miroslav M. and Pavelkić, Vesna M. and Marinković, Miloš",
year = "2000",
abstract = "The effect of easily ionized elements (EIE) in d.c. plasma (DCP) has been modeled and experimentally investigated. The introduction of the EIEs in the U-shaped DCP decreases a potential barrier due to an internal radial electric field, which allows the partially ionized analyte better entry into the hot plasma zone and produces enhancement of the analyte spectral emission. Compared to the equilibrium concentration, the increased electron concentration in the fringe region due to large radial gradients is accounted for in the model. By comparing model predictions to experimental data, the validity of the model is tested. The main features of the effect, the large enhancement at small addition of EIE and almost equal enhancement of ion and atom line intensities, are fairly well described by the model. The results are believed to be applicable to the inverted Y-shaped DCP. The effect in the inductively coupled plasma (ICP) has been briefly discussed from the point of view of the proposed model. (C) 2000 Elsevier Science B.V. All rights reserved.",
journal = "Spectrochimica Acta. Part B: Atomic Spectroscopy",
title = "The role of demixing effect in analyte emission enhancement by easily ionized elements in d.c. plasma",
volume = "55",
number = "8",
pages = "1373-1384",
doi = "10.1016/S0584-8547(00)00242-1"
}

Pavlović, M. S., Kuzmanović, M. M., Pavelkić, V. M.,& Marinković, M.. (2000). The role of demixing effect in analyte emission enhancement by easily ionized elements in d.c. plasma. in Spectrochimica Acta. Part B: Atomic Spectroscopy, 55(8), 1373-1384.
https://doi.org/10.1016/S0584-8547(00)00242-1

Pavlović MS, Kuzmanović MM, Pavelkić VM, Marinković M. The role of demixing effect in analyte emission enhancement by easily ionized elements in d.c. plasma. in Spectrochimica Acta. Part B: Atomic Spectroscopy. 2000;55(8):1373-1384.
doi:10.1016/S0584-8547(00)00242-1 .

Pavlović, Mirjana S., Kuzmanović, Miroslav M., Pavelkić, Vesna M., Marinković, Miloš, "The role of demixing effect in analyte emission enhancement by easily ionized elements in d.c. plasma" in Spectrochimica Acta. Part B: Atomic Spectroscopy, 55, no. 8 (2000):1373-1384,
https://doi.org/10.1016/S0584-8547(00)00242-1 . .