TY  - JOUR
AU  - Simonović, Mladen
AU  - Milošević-Zlatanović, Svetlana
AU  - Milosavić, Nenad
AU  - Vrvić, Miroslav
AU  - Simonović, Branislav
PY  - 2009
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3414
AB  - Diverse recombinant immunoreagents specific for TNT–derivatives were tested in different assay forms in order to analyze their specificity and sensitivity. Performance of immunoassays was based on TNP–protein conjugates immobilization on a solid surface. In this work, the detection limit for TNT–analog TNP–Tris was 250 fmol or 87 pg mL−1 (87 ppt), which represents the most sensitive assay published until now, regarding the detection of recombinant antibodies.
PB  - Versita
T2  - Chemical Papers
T1  - Characterization of recombinant antibodies for detection of TNT and its derivatives
VL  - 63
IS  - 4
SP  - 391
EP  - 398
DO  - 10.2478/s11696-009-0043-5
ER  - 

@article{
author = "Simonović, Mladen and Milošević-Zlatanović, Svetlana and Milosavić, Nenad and Vrvić, Miroslav and Simonović, Branislav",
year = "2009",
abstract = "Diverse recombinant immunoreagents specific for TNT–derivatives were tested in different assay forms in order to analyze their specificity and sensitivity. Performance of immunoassays was based on TNP–protein conjugates immobilization on a solid surface. In this work, the detection limit for TNT–analog TNP–Tris was 250 fmol or 87 pg mL−1 (87 ppt), which represents the most sensitive assay published until now, regarding the detection of recombinant antibodies.",
publisher = "Versita",
journal = "Chemical Papers",
title = "Characterization of recombinant antibodies for detection of TNT and its derivatives",
volume = "63",
number = "4",
pages = "391-398",
doi = "10.2478/s11696-009-0043-5"
}

Simonović, M., Milošević-Zlatanović, S., Milosavić, N., Vrvić, M.,& Simonović, B.. (2009). Characterization of recombinant antibodies for detection of TNT and its derivatives. in Chemical Papers
Versita., 63(4), 391-398.
https://doi.org/10.2478/s11696-009-0043-5

Simonović M, Milošević-Zlatanović S, Milosavić N, Vrvić M, Simonović B. Characterization of recombinant antibodies for detection of TNT and its derivatives. in Chemical Papers. 2009;63(4):391-398.
doi:10.2478/s11696-009-0043-5 .

Simonović, Mladen, Milošević-Zlatanović, Svetlana, Milosavić, Nenad, Vrvić, Miroslav, Simonović, Branislav, "Characterization of recombinant antibodies for detection of TNT and its derivatives" in Chemical Papers, 63, no. 4 (2009):391-398,
https://doi.org/10.2478/s11696-009-0043-5 . .

TY  - JOUR
AU  - Bogdanović-Pristov, Jelena J.
AU  - Milosavić, Nenad B.
AU  - Prodanović, Radivoje M.
AU  - Dučić, Tanja
AU  - Radotić, Ksenija
PY  - 2007
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4334
AB  - Variations were studied of the activity and isoenzyme patterns of soluble peroxidase, catalase, catechol oxidase and superoxide dismutase, in needles of the Balkan endemic conifer Serbian spruce, Picea omorika (Panč.) Purkinye. The samples were collected from the natural habitat of the species, Mt. Tara. Seasonal changes were found to affect enzymatic activities and isoenzyme profiles. Total protein content was significantly lower in the summer than in other seasons. Several isoforms of peroxidase, catechol oxidase and superoxide dismutase (SOD), as well as two catalase isoenzymes were detected. The number of peroxidase isoenzymes was greatest during the vegetative season. Catalase and catechol oxidase peaked in summer and spring, respectively. Total SOD and Mn-SOD activities were significantly higher in the winter samples than the summer ones.
PB  - Elsevier
T2  - Biochemical Systematics and Ecology
T1  - Variability of antioxidant enzyme activity and isoenzyme profile in needles of Serbian spruce (Picea omorika (Panč.) Purkinye)
VL  - 35
IS  - 5
SP  - 263
EP  - 273
DO  - 10.1016/j.bse.2006.12.001
ER  - 

@article{
author = "Bogdanović-Pristov, Jelena J. and Milosavić, Nenad B. and Prodanović, Radivoje M. and Dučić, Tanja and Radotić, Ksenija",
year = "2007",
abstract = "Variations were studied of the activity and isoenzyme patterns of soluble peroxidase, catalase, catechol oxidase and superoxide dismutase, in needles of the Balkan endemic conifer Serbian spruce, Picea omorika (Panč.) Purkinye. The samples were collected from the natural habitat of the species, Mt. Tara. Seasonal changes were found to affect enzymatic activities and isoenzyme profiles. Total protein content was significantly lower in the summer than in other seasons. Several isoforms of peroxidase, catechol oxidase and superoxide dismutase (SOD), as well as two catalase isoenzymes were detected. The number of peroxidase isoenzymes was greatest during the vegetative season. Catalase and catechol oxidase peaked in summer and spring, respectively. Total SOD and Mn-SOD activities were significantly higher in the winter samples than the summer ones.",
publisher = "Elsevier",
journal = "Biochemical Systematics and Ecology",
title = "Variability of antioxidant enzyme activity and isoenzyme profile in needles of Serbian spruce (Picea omorika (Panč.) Purkinye)",
volume = "35",
number = "5",
pages = "263-273",
doi = "10.1016/j.bse.2006.12.001"
}

Bogdanović-Pristov, J. J., Milosavić, N. B., Prodanović, R. M., Dučić, T.,& Radotić, K.. (2007). Variability of antioxidant enzyme activity and isoenzyme profile in needles of Serbian spruce (Picea omorika (Panč.) Purkinye). in Biochemical Systematics and Ecology
Elsevier., 35(5), 263-273.
https://doi.org/10.1016/j.bse.2006.12.001

Bogdanović-Pristov JJ, Milosavić NB, Prodanović RM, Dučić T, Radotić K. Variability of antioxidant enzyme activity and isoenzyme profile in needles of Serbian spruce (Picea omorika (Panč.) Purkinye). in Biochemical Systematics and Ecology. 2007;35(5):263-273.
doi:10.1016/j.bse.2006.12.001 .

Bogdanović-Pristov, Jelena J., Milosavić, Nenad B., Prodanović, Radivoje M., Dučić, Tanja, Radotić, Ksenija, "Variability of antioxidant enzyme activity and isoenzyme profile in needles of Serbian spruce (Picea omorika (Panč.) Purkinye)" in Biochemical Systematics and Ecology, 35, no. 5 (2007):263-273,
https://doi.org/10.1016/j.bse.2006.12.001 . .

TY  - JOUR
AU  - Milosavić, Nenad B.
AU  - Prodanović, Radivoje
AU  - Jovanović, Slobodan M.
AU  - Vujčić, Zoran
PY  - 2007
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4264
AB  - We succeeded in the immobilization of 190 mg of periodate oxidized glucoamylase per gram of macroporous polymer. The covalently immobilized enzyme had a specific activity of 1100 U/g. The temperature and pH optimum as well as kinetic parameters were determined. The immobilized enzyme was tested in different types of reactors for hydrolysis of concentrated maltose and starch hydrolysate syrups. The DE value of 98.6, obtained the immobilized enzyme, was slightly higher than that for the soluble form, when acting on 20% substrates.During continuous use in a packed bed reactor over a period of 4 weeks the immobilized enzyme produced 1300 kg of glucose per 1 L of reactor volume without any decrease in its activity.
PB  - Elsevier
T2  - Enzyme and Microbial Technology
T1  - Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA)
VL  - 40
IS  - 5
SP  - 1422
EP  - 1426
DO  - 10.1016/j.enzmictec.2006.10.018
ER  - 

@article{
author = "Milosavić, Nenad B. and Prodanović, Radivoje and Jovanović, Slobodan M. and Vujčić, Zoran",
year = "2007",
abstract = "We succeeded in the immobilization of 190 mg of periodate oxidized glucoamylase per gram of macroporous polymer. The covalently immobilized enzyme had a specific activity of 1100 U/g. The temperature and pH optimum as well as kinetic parameters were determined. The immobilized enzyme was tested in different types of reactors for hydrolysis of concentrated maltose and starch hydrolysate syrups. The DE value of 98.6, obtained the immobilized enzyme, was slightly higher than that for the soluble form, when acting on 20% substrates.During continuous use in a packed bed reactor over a period of 4 weeks the immobilized enzyme produced 1300 kg of glucose per 1 L of reactor volume without any decrease in its activity.",
publisher = "Elsevier",
journal = "Enzyme and Microbial Technology",
title = "Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA)",
volume = "40",
number = "5",
pages = "1422-1426",
doi = "10.1016/j.enzmictec.2006.10.018"
}

Milosavić, N. B., Prodanović, R., Jovanović, S. M.,& Vujčić, Z.. (2007). Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA). in Enzyme and Microbial Technology
Elsevier., 40(5), 1422-1426.
https://doi.org/10.1016/j.enzmictec.2006.10.018

Milosavić NB, Prodanović R, Jovanović SM, Vujčić Z. Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA). in Enzyme and Microbial Technology. 2007;40(5):1422-1426.
doi:10.1016/j.enzmictec.2006.10.018 .

Milosavić, Nenad B., Prodanović, Radivoje, Jovanović, Slobodan M., Vujčić, Zoran, "Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA)" in Enzyme and Microbial Technology, 40, no. 5 (2007):1422-1426,
https://doi.org/10.1016/j.enzmictec.2006.10.018 . .

TY  - JOUR
AU  - Ahmedi, Khaled S. O. H
AU  - Milosavić, Nenad
AU  - Popović, Milica
AU  - Prodanović, Radivoje M.
AU  - Knežević-Jugović, Zorica D.
AU  - Jankov, Ratko M.
PY  - 2007
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4302
AB  - α-Glucosidase from S. cerevisiae was covalently immobilized onto Sepabeads EC-EA by the glutaraldehyde method. An analysis of the variables controlling the immobilization process is first presented and it is shown that the highest coupling of α-glucosidase occurred within 24 h. Also, a loading of 30 mg/g support proved to be effective, resulting in a rather high activity of around 45 U g-1 with a satisfactory degree of enzyme fixed. Both free and immobilized enzymes were then characterized by determining the activity profile as a function of pH, temperature and thermal stability. The obtained immobilized preparation showed the same optimum pH, but a higher optimum temperature compared with the soluble one. In addition, the immobilized enzyme treated at 45°C for 1 h still retained an activity of around 20 %, whereas the free enzyme completely lost its original activity under this condition. In conclusion, the developed immobilization procedure is quite simple, easily reproducible and provides a promising solution for the application of immobilized α-glucosidase.
AB  - Малтаза из S. cerevisiae је ковалентно имобилизована на Sepabeads EC-EA након акти-
вације носача раствором глутаралдехида. Испитивањем кинетике имобилизације утврђено је
да се 25 % ензима имобилизује након 24 часа. Имобилизована α-глукозидаза има исти pH
оптимум као и растворни ензим, док је оптимална температура за активност имобилизованог
ензима увећана за 10 °C у поређењу са растворним ензимом. Када се упореде заостале
активности растворне и имобилизоване форме α-глукозидазе, након инкубације од 1 h на
α- 45 °C растворни ензим не показује активност док имобилизована форма задржава око 20 %
почeтне активности. Имобилизована форма ензима задржава 20 % почетне активности чак и
после 3 h инкубације на 45 °C.
PB  - Belgrade : Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae
T1  - Добијање и  проучавање имобилизације  α-глукозидазе из пекарског квасца Saccharomyces cerevisiae
VL  - 72
IS  - 12
SP  - 1255
EP  - 1263
DO  - 10.2298/JSC0712255A
ER  - 

@article{
author = "Ahmedi, Khaled S. O. H and Milosavić, Nenad and Popović, Milica and Prodanović, Radivoje M. and Knežević-Jugović, Zorica D. and Jankov, Ratko M.",
year = "2007",
abstract = "α-Glucosidase from S. cerevisiae was covalently immobilized onto Sepabeads EC-EA by the glutaraldehyde method. An analysis of the variables controlling the immobilization process is first presented and it is shown that the highest coupling of α-glucosidase occurred within 24 h. Also, a loading of 30 mg/g support proved to be effective, resulting in a rather high activity of around 45 U g-1 with a satisfactory degree of enzyme fixed. Both free and immobilized enzymes were then characterized by determining the activity profile as a function of pH, temperature and thermal stability. The obtained immobilized preparation showed the same optimum pH, but a higher optimum temperature compared with the soluble one. In addition, the immobilized enzyme treated at 45°C for 1 h still retained an activity of around 20 %, whereas the free enzyme completely lost its original activity under this condition. In conclusion, the developed immobilization procedure is quite simple, easily reproducible and provides a promising solution for the application of immobilized α-glucosidase., Малтаза из S. cerevisiae је ковалентно имобилизована на Sepabeads EC-EA након акти-
вације носача раствором глутаралдехида. Испитивањем кинетике имобилизације утврђено је
да се 25 % ензима имобилизује након 24 часа. Имобилизована α-глукозидаза има исти pH
оптимум као и растворни ензим, док је оптимална температура за активност имобилизованог
ензима увећана за 10 °C у поређењу са растворним ензимом. Када се упореде заостале
активности растворне и имобилизоване форме α-глукозидазе, након инкубације од 1 h на
α- 45 °C растворни ензим не показује активност док имобилизована форма задржава око 20 %
почeтне активности. Имобилизована форма ензима задржава 20 % почетне активности чак и
после 3 h инкубације на 45 °C.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae, Добијање и  проучавање имобилизације  α-глукозидазе из пекарског квасца Saccharomyces cerevisiae",
volume = "72",
number = "12",
pages = "1255-1263",
doi = "10.2298/JSC0712255A"
}

Ahmedi, K. S. O. H., Milosavić, N., Popović, M., Prodanović, R. M., Knežević-Jugović, Z. D.,& Jankov, R. M.. (2007). Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae. in Journal of the Serbian Chemical Society
Belgrade : Serbian Chemical Society., 72(12), 1255-1263.
https://doi.org/10.2298/JSC0712255A

Ahmedi KSOH, Milosavić N, Popović M, Prodanović RM, Knežević-Jugović ZD, Jankov RM. Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae. in Journal of the Serbian Chemical Society. 2007;72(12):1255-1263.
doi:10.2298/JSC0712255A .

Ahmedi, Khaled S. O. H, Milosavić, Nenad, Popović, Milica, Prodanović, Radivoje M., Knežević-Jugović, Zorica D., Jankov, Ratko M., "Preparation and studies on immobilized alpha-glucosidase from baker's yeast Saccharomyces cerevisiae" in Journal of the Serbian Chemical Society, 72, no. 12 (2007):1255-1263,
https://doi.org/10.2298/JSC0712255A . .

TY  - JOUR
AU  - Milosavic, N
AU  - Prodanović, Radivoje
AU  - Jovanovic, S.
AU  - Novaković, Irena
AU  - Vujčić, Zoran
PY  - 2005
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/205
AB  - Amyloglucosidase from A. niger was covalently immobilized onto poly( GMA-co-EGDMA) by the glutaraldehyde and periodate method. The immobilization of amyloglucosidase after periodate oxidation gave a preparate with the highest specific activity reported so far on similar polymers. The obtained immobilized preparates show the same pH optimum, but a higher temperature optimum compared with the soluble enzyme. The kinetic parameters for the hydrolysis of soluble starch by free and both immobilized enzymes were determined.
AB  - Amiloglukozidaza iz A.niger je imobilizovana na poly(GMA-co-EGDMA) glutaraldehidnom i perjodatnom metodom. Imobilizacija amiloglukozidaze nakon perjodatne oksidacije daje preparat sa najvećom do sada objavljenom specifičnom aktivnosti na sličnim polimerima. Dobijeni imobilizovani preparat ima isti pH optimum ali povećani termooptimum u poređenju sa rastvornim enzimom. Određeni su i kinetički parametri za hidrolizu rastvornog skroba imobilizovanim kao i rastvornim enzimom.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Preparation and characterization of two types of covalently immobilized amyloglucosidase
T1  - Dobijanje i karakterizacija dva tipa imobilizovane amiloglukozidaze
VL  - 70
IS  - 5
SP  - 713
EP  - 719
DO  - 10.2298/JSC0505713M
ER  - 

@article{
author = "Milosavic, N and Prodanović, Radivoje and Jovanovic, S. and Novaković, Irena and Vujčić, Zoran",
year = "2005",
abstract = "Amyloglucosidase from A. niger was covalently immobilized onto poly( GMA-co-EGDMA) by the glutaraldehyde and periodate method. The immobilization of amyloglucosidase after periodate oxidation gave a preparate with the highest specific activity reported so far on similar polymers. The obtained immobilized preparates show the same pH optimum, but a higher temperature optimum compared with the soluble enzyme. The kinetic parameters for the hydrolysis of soluble starch by free and both immobilized enzymes were determined., Amiloglukozidaza iz A.niger je imobilizovana na poly(GMA-co-EGDMA) glutaraldehidnom i perjodatnom metodom. Imobilizacija amiloglukozidaze nakon perjodatne oksidacije daje preparat sa najvećom do sada objavljenom specifičnom aktivnosti na sličnim polimerima. Dobijeni imobilizovani preparat ima isti pH optimum ali povećani termooptimum u poređenju sa rastvornim enzimom. Određeni su i kinetički parametri za hidrolizu rastvornog skroba imobilizovanim kao i rastvornim enzimom.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Preparation and characterization of two types of covalently immobilized amyloglucosidase, Dobijanje i karakterizacija dva tipa imobilizovane amiloglukozidaze",
volume = "70",
number = "5",
pages = "713-719",
doi = "10.2298/JSC0505713M"
}

Milosavic, N., Prodanović, R., Jovanovic, S., Novaković, I.,& Vujčić, Z.. (2005). Preparation and characterization of two types of covalently immobilized amyloglucosidase. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 70(5), 713-719.
https://doi.org/10.2298/JSC0505713M

Milosavic N, Prodanović R, Jovanovic S, Novaković I, Vujčić Z. Preparation and characterization of two types of covalently immobilized amyloglucosidase. in Journal of the Serbian Chemical Society. 2005;70(5):713-719.
doi:10.2298/JSC0505713M .

Milosavic, N, Prodanović, Radivoje, Jovanovic, S., Novaković, Irena, Vujčić, Zoran, "Preparation and characterization of two types of covalently immobilized amyloglucosidase" in Journal of the Serbian Chemical Society, 70, no. 5 (2005):713-719,
https://doi.org/10.2298/JSC0505713M . .

TY  - JOUR
AU  - Bezbradica, Dejan I.
AU  - Ćorović, Jasmina J.
AU  - Prodanović, Radivoje
AU  - Milosavić, Nenad B.
AU  - Knežević, Zorica D.
PY  - 2005
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2686
AB  - An approach is presented for the stable covalent immobilization of Upase from Candida rugosa on Eupergit® with a high retention of hydrolytic activity. It comprises covalent bonding via lipase carbohydrate moiety previously modified by periodate oxidation, allowing a reduction in the involvement of the enzyme functional groups that are probably important in the catalytic mechanism. The hydrolytic activities of the lipase immobilized on Eupergif1 by two conventional methods (via oxirane group and via glutaralde-hyde) and with periodate method were compared. Results of lipase assays suggest that periodate method is superior for lipase immobilization on Eupergit® among methods applied in this study with respect to both, yield of immobilization and hydrolytic activity of the immobilized enzyme.
AB  - U ovom radu je ispitana mogućnost primene metode za kovalentno vezivanje lipaze iz Candida rugosa za komercijalni polimerni nosač Eupergit® kojom se dobijaju stabilni i aktivni imobilisani enzimi. Vezivanje se odvija preko ugljenohidratne komponente enzima, koja je prethodno modifikovana oksidacijom pomoću perjodata, a ne preko proteinske komponente, koja je važna za katalitičku aktivnost enzima. Hidrolitička aktivnost na ovaj način imobilisane lipaze upoređena je sa aktivnostima lipaza koje su imobilisane pomoću dve konvencionalne metode (vezivanje preko epoksidnih grupa nosača i vezivanje za nosač modifikovan glutaraldehidom). Rezultati ovog istraživanja pokazuju da je perjodatna metoda pogodnija za imobilizaciju lipaze na Eupergit® sa oba ispitivana aspekta: prinosa imobilizacije i hidrolitičke aktivnosti imobilisanog enzima.
T2  - Acta periodica technologica
T1  - Covalent immobilization of lipase from Candida rugosa on Eupergit®
T1  - Kovalentna imobilizacija lipaze iz Candida rugosa za Eupergit®
IS  - 36
SP  - 179
EP  - 186
DO  - 10.2298/APT0536179B
ER  - 

@article{
author = "Bezbradica, Dejan I. and Ćorović, Jasmina J. and Prodanović, Radivoje and Milosavić, Nenad B. and Knežević, Zorica D.",
year = "2005",
abstract = "An approach is presented for the stable covalent immobilization of Upase from Candida rugosa on Eupergit® with a high retention of hydrolytic activity. It comprises covalent bonding via lipase carbohydrate moiety previously modified by periodate oxidation, allowing a reduction in the involvement of the enzyme functional groups that are probably important in the catalytic mechanism. The hydrolytic activities of the lipase immobilized on Eupergif1 by two conventional methods (via oxirane group and via glutaralde-hyde) and with periodate method were compared. Results of lipase assays suggest that periodate method is superior for lipase immobilization on Eupergit® among methods applied in this study with respect to both, yield of immobilization and hydrolytic activity of the immobilized enzyme., U ovom radu je ispitana mogućnost primene metode za kovalentno vezivanje lipaze iz Candida rugosa za komercijalni polimerni nosač Eupergit® kojom se dobijaju stabilni i aktivni imobilisani enzimi. Vezivanje se odvija preko ugljenohidratne komponente enzima, koja je prethodno modifikovana oksidacijom pomoću perjodata, a ne preko proteinske komponente, koja je važna za katalitičku aktivnost enzima. Hidrolitička aktivnost na ovaj način imobilisane lipaze upoređena je sa aktivnostima lipaza koje su imobilisane pomoću dve konvencionalne metode (vezivanje preko epoksidnih grupa nosača i vezivanje za nosač modifikovan glutaraldehidom). Rezultati ovog istraživanja pokazuju da je perjodatna metoda pogodnija za imobilizaciju lipaze na Eupergit® sa oba ispitivana aspekta: prinosa imobilizacije i hidrolitičke aktivnosti imobilisanog enzima.",
journal = "Acta periodica technologica",
title = "Covalent immobilization of lipase from Candida rugosa on Eupergit®, Kovalentna imobilizacija lipaze iz Candida rugosa za Eupergit®",
number = "36",
pages = "179-186",
doi = "10.2298/APT0536179B"
}

Bezbradica, D. I., Ćorović, J. J., Prodanović, R., Milosavić, N. B.,& Knežević, Z. D.. (2005). Covalent immobilization of lipase from Candida rugosa on Eupergit®. in Acta periodica technologica(36), 179-186.
https://doi.org/10.2298/APT0536179B

Bezbradica DI, Ćorović JJ, Prodanović R, Milosavić NB, Knežević ZD. Covalent immobilization of lipase from Candida rugosa on Eupergit®. in Acta periodica technologica. 2005;(36):179-186.
doi:10.2298/APT0536179B .

Bezbradica, Dejan I., Ćorović, Jasmina J., Prodanović, Radivoje, Milosavić, Nenad B., Knežević, Zorica D., "Covalent immobilization of lipase from Candida rugosa on Eupergit®" in Acta periodica technologica, no. 36 (2005):179-186,
https://doi.org/10.2298/APT0536179B . .

TY  - JOUR
AU  - Milosavić, Nenad B.
AU  - Prodanović, Radivoje
PY  - 2004
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2683
AB  - The discovery of porosome and elucidation of its morphology, dynamics, and composition, reveled where membrane-bound secretory vesicles dock and fuse to release their contents. How membrane-bounded secretori vesicles fuse at plasa membrane-associated porosome has also been eluciated. This discovery has also revealed how little we know about the cell, and thus heralds a new revolution in cell biology, i.e. the birth of nano cell biology.
T2  - Hemijski pregled
T1  - Porosom: A new cell structure
T1  - Porozom - nova ćelijska struktura
VL  - 45
IS  - 5
SP  - 102
EP  - 103
UR  - https://hdl.handle.net/21.15107/rcub_cer_2683
ER  - 

@article{
author = "Milosavić, Nenad B. and Prodanović, Radivoje",
year = "2004",
abstract = "The discovery of porosome and elucidation of its morphology, dynamics, and composition, reveled where membrane-bound secretory vesicles dock and fuse to release their contents. How membrane-bounded secretori vesicles fuse at plasa membrane-associated porosome has also been eluciated. This discovery has also revealed how little we know about the cell, and thus heralds a new revolution in cell biology, i.e. the birth of nano cell biology.",
journal = "Hemijski pregled",
title = "Porosom: A new cell structure, Porozom - nova ćelijska struktura",
volume = "45",
number = "5",
pages = "102-103",
url = "https://hdl.handle.net/21.15107/rcub_cer_2683"
}

Milosavić, N. B.,& Prodanović, R.. (2004). Porosom: A new cell structure. in Hemijski pregled, 45(5), 102-103.
https://hdl.handle.net/21.15107/rcub_cer_2683

Milosavić NB, Prodanović R. Porosom: A new cell structure. in Hemijski pregled. 2004;45(5):102-103.
https://hdl.handle.net/21.15107/rcub_cer_2683 .

Milosavić, Nenad B., Prodanović, Radivoje, "Porosom: A new cell structure" in Hemijski pregled, 45, no. 5 (2004):102-103,
https://hdl.handle.net/21.15107/rcub_cer_2683 .

TY  - JOUR
AU  - Novaković, Irena
AU  - Vujčić, Zoran
AU  - Božić, Tatjana T.
AU  - Božić, Nataša
AU  - Milosavić, Nenad B.
AU  - Sladić, Dušan
PY  - 2003
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/118
AB  - The avarone/avarol quinone/hydroquinone couple, as well as their derivatives show considerable antitumor activity. In this work, covalent modifications of β-lactoglobulin, isolated from cow milk, by avarone, its model compound 2-tert-butyl-1,4-benzoquinone, and several of their alkylthio derivatives were studied. The techniques applied for assaying the modifications were UV/VIS spectrophotometry, SDS PAGE and isoelectrofocusing. The results of the SDS PAGE suggest that polymerisation of the protein occurs. The shift of the pI of the protein upon modification toward lower values indicates that lysine amino groups are the principal site of the reaction of β-lactoglobulin with the quinines.
AB  - Hinonsko/hidrohinonski par avaron/avarol i njihovi derivati pokazuju značajnu antitumorsku aktivnost. U ovom radu proučavane su kovalentne modifikacije β-laktoglobulina, izolovanog iz kravljeg mleka, avaronom, njegovim model-jedinjenjem 2-tert-butil-1,4-benzohinonom i njihovim alkiltio-derivatima. Za ispitivanje modifikacija korišćene su UV/VIS spektrofotometrija, SDS PAGE i izoelektrofokusiranje. Rezultat SDS PAGE ukazuje da se protein polimerizuje. Pomeranje pI vrednosti proteina nakon modifikacije ka nižim vrednostima pokazuje da su amino grupe lizina glavna mesta reakcije β-laktoglobulina sa hinonima.
PB  - Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Chemical modification of β-lactoglobulin by quinines
T1  - Hemijske modifikacije β-laktoglobulina hinonima
VL  - 68
IS  - 4-5
SP  - 243
EP  - 248
DO  - 10.2298/JSC0305243N
ER  - 

@article{
author = "Novaković, Irena and Vujčić, Zoran and Božić, Tatjana T. and Božić, Nataša and Milosavić, Nenad B. and Sladić, Dušan",
year = "2003",
abstract = "The avarone/avarol quinone/hydroquinone couple, as well as their derivatives show considerable antitumor activity. In this work, covalent modifications of β-lactoglobulin, isolated from cow milk, by avarone, its model compound 2-tert-butyl-1,4-benzoquinone, and several of their alkylthio derivatives were studied. The techniques applied for assaying the modifications were UV/VIS spectrophotometry, SDS PAGE and isoelectrofocusing. The results of the SDS PAGE suggest that polymerisation of the protein occurs. The shift of the pI of the protein upon modification toward lower values indicates that lysine amino groups are the principal site of the reaction of β-lactoglobulin with the quinines., Hinonsko/hidrohinonski par avaron/avarol i njihovi derivati pokazuju značajnu antitumorsku aktivnost. U ovom radu proučavane su kovalentne modifikacije β-laktoglobulina, izolovanog iz kravljeg mleka, avaronom, njegovim model-jedinjenjem 2-tert-butil-1,4-benzohinonom i njihovim alkiltio-derivatima. Za ispitivanje modifikacija korišćene su UV/VIS spektrofotometrija, SDS PAGE i izoelektrofokusiranje. Rezultat SDS PAGE ukazuje da se protein polimerizuje. Pomeranje pI vrednosti proteina nakon modifikacije ka nižim vrednostima pokazuje da su amino grupe lizina glavna mesta reakcije β-laktoglobulina sa hinonima.",
publisher = "Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Chemical modification of β-lactoglobulin by quinines, Hemijske modifikacije β-laktoglobulina hinonima",
volume = "68",
number = "4-5",
pages = "243-248",
doi = "10.2298/JSC0305243N"
}

Novaković, I., Vujčić, Z., Božić, T. T., Božić, N., Milosavić, N. B.,& Sladić, D.. (2003). Chemical modification of β-lactoglobulin by quinines. in Journal of the Serbian Chemical Society
Serbian Chemical Society., 68(4-5), 243-248.
https://doi.org/10.2298/JSC0305243N

Novaković I, Vujčić Z, Božić TT, Božić N, Milosavić NB, Sladić D. Chemical modification of β-lactoglobulin by quinines. in Journal of the Serbian Chemical Society. 2003;68(4-5):243-248.
doi:10.2298/JSC0305243N .

Novaković, Irena, Vujčić, Zoran, Božić, Tatjana T., Božić, Nataša, Milosavić, Nenad B., Sladić, Dušan, "Chemical modification of β-lactoglobulin by quinines" in Journal of the Serbian Chemical Society, 68, no. 4-5 (2003):243-248,
https://doi.org/10.2298/JSC0305243N . .