TY  - JOUR
AU  - Dojnov, Biljana
AU  - Pavlović, Ratko
AU  - Bozić, Natasa M
AU  - Margetić, Aleksandra
AU  - Nenadović, Vera
AU  - Ivanović, Jelisaveta
AU  - Vujčić, Zoran M.
PY  - 2013
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/1026
AB  - The influence of diet composition - two substrates, wheat bran and sawdust - on isoform expression of digestive enzymes (cellulase, amylase and peptidase) in the midgut of Morimus funereus larvae was examined. Their impact on larval development was demonstrated by measuring the increase of larval weight during development and by analysis of digestive enzymes zymographic profiles, where the expression of cellulase isoforms from M. funereus larvae midgut has been examined for the first time in this study. Larvae reared on wheat bran had higher body weight between day 60 and day 100 than larvae reared on sawdust; however, both groups achieved similar body weight after day 110. Wheat bran as substrate induced different cellulase and amylase isoforms. Oak sawdust in substrate acted as inducer of peptidases. The highest cellulase activity and the greatest isoform variability were detected in the midgut extracts of larvae reared on wheat bran. From our results it can be assumed that M. funereus endocellulase, amylase and peptidase are secreted in the anterior midgut, and their concentration gradually decreases towards the hindgut (C) 2013 Elsevier Inc. All rights reserved.
T2  - Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology
T1  - Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition
IS  - 4
VL  - 164
SP  - 183
EP  - 267
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_1026
ER  - 

@article{
author = "Dojnov, Biljana and Pavlović, Ratko and Bozić, Natasa M and Margetić, Aleksandra and Nenadović, Vera and Ivanović, Jelisaveta and Vujčić, Zoran M.",
year = "2013",
abstract = "The influence of diet composition - two substrates, wheat bran and sawdust - on isoform expression of digestive enzymes (cellulase, amylase and peptidase) in the midgut of Morimus funereus larvae was examined. Their impact on larval development was demonstrated by measuring the increase of larval weight during development and by analysis of digestive enzymes zymographic profiles, where the expression of cellulase isoforms from M. funereus larvae midgut has been examined for the first time in this study. Larvae reared on wheat bran had higher body weight between day 60 and day 100 than larvae reared on sawdust; however, both groups achieved similar body weight after day 110. Wheat bran as substrate induced different cellulase and amylase isoforms. Oak sawdust in substrate acted as inducer of peptidases. The highest cellulase activity and the greatest isoform variability were detected in the midgut extracts of larvae reared on wheat bran. From our results it can be assumed that M. funereus endocellulase, amylase and peptidase are secreted in the anterior midgut, and their concentration gradually decreases towards the hindgut (C) 2013 Elsevier Inc. All rights reserved.",
journal = "Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology",
title = "Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition",
number = "4",
volume = "164",
pages = "183-267",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_1026"
}

Dojnov, B., Pavlović, R., Bozić, N. M., Margetić, A., Nenadović, V., Ivanović, J.,& Vujčić, Z. M.. (2013). Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition. in Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology, 164(4), 183-267.
https://hdl.handle.net/21.15107/rcub_ibiss_1026

Dojnov B, Pavlović R, Bozić NM, Margetić A, Nenadović V, Ivanović J, Vujčić ZM. Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition. in Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology. 2013;164(4):183-267.
https://hdl.handle.net/21.15107/rcub_ibiss_1026 .

Dojnov, Biljana, Pavlović, Ratko, Bozić, Natasa M, Margetić, Aleksandra, Nenadović, Vera, Ivanović, Jelisaveta, Vujčić, Zoran M., "Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition" in Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology, 164, no. 4 (2013):183-267,
https://hdl.handle.net/21.15107/rcub_ibiss_1026 .

TY  - JOUR
AU  - Pavlović, R.
AU  - Grujić, Marica
AU  - Dojnov, Biljana
AU  - Vujčić, Miroslava T.
AU  - Nenadović, Vera
AU  - Ivanović, Jelisaveta
AU  - Vujčić, Zoran M.
PY  - 2012
PY  - 2012
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/310
AB  - The expression and distribution of digestive cellulases along the midgut of Cerambyx cerdo larvae were analyzed for the first time and are presented in this article. Four groups of larvae were examined: larvae developed in the wild; larvae taken from the wild and successively reared on an artificial diet based on polenta; and larvae hatched in the laboratory and reared on two different artificial diets. Seven endocellulase and seven β-D-glucosidase isoforms were detected in all midgut extracts of C. cerdo with a zymogram after native PAGE. We observed that C. cerdo larvae are capable of producing cellulase isoforms with different PAGE mobilities depending on the nutrient substrate. From our findings it can be assumed that, depending on the distribution of endocellulase and β-D-glucosidase, cellulose molecules are first fragmented in the anterior and middle midgut by endo-β-1,4-glucanase; subsequently, the obtained fragments are broken down by β-D-glucosidase mostly in middle midgut.
T2  - Archives of Biological Sciences
T1  - Influence of nutrient substrates on the expression of cellulases in Cerambyx cerdo L. (Coleoptera: Cerambycidae) larvae
IS  - 2
VL  - 64
SP  - 757
EP  - 765
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_310
ER  - 

@article{
author = "Pavlović, R. and Grujić, Marica and Dojnov, Biljana and Vujčić, Miroslava T. and Nenadović, Vera and Ivanović, Jelisaveta and Vujčić, Zoran M.",
year = "2012, 2012",
abstract = "The expression and distribution of digestive cellulases along the midgut of Cerambyx cerdo larvae were analyzed for the first time and are presented in this article. Four groups of larvae were examined: larvae developed in the wild; larvae taken from the wild and successively reared on an artificial diet based on polenta; and larvae hatched in the laboratory and reared on two different artificial diets. Seven endocellulase and seven β-D-glucosidase isoforms were detected in all midgut extracts of C. cerdo with a zymogram after native PAGE. We observed that C. cerdo larvae are capable of producing cellulase isoforms with different PAGE mobilities depending on the nutrient substrate. From our findings it can be assumed that, depending on the distribution of endocellulase and β-D-glucosidase, cellulose molecules are first fragmented in the anterior and middle midgut by endo-β-1,4-glucanase; subsequently, the obtained fragments are broken down by β-D-glucosidase mostly in middle midgut.",
journal = "Archives of Biological Sciences",
title = "Influence of nutrient substrates on the expression of cellulases in Cerambyx cerdo L. (Coleoptera: Cerambycidae) larvae",
number = "2",
volume = "64",
pages = "757-765",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_310"
}

Pavlović, R., Grujić, M., Dojnov, B., Vujčić, M. T., Nenadović, V., Ivanović, J.,& Vujčić, Z. M.. (2012). Influence of nutrient substrates on the expression of cellulases in Cerambyx cerdo L. (Coleoptera: Cerambycidae) larvae. in Archives of Biological Sciences, 64(2), 757-765.
https://hdl.handle.net/21.15107/rcub_ibiss_310

Pavlović R, Grujić M, Dojnov B, Vujčić MT, Nenadović V, Ivanović J, Vujčić ZM. Influence of nutrient substrates on the expression of cellulases in Cerambyx cerdo L. (Coleoptera: Cerambycidae) larvae. in Archives of Biological Sciences. 2012;64(2):757-765.
https://hdl.handle.net/21.15107/rcub_ibiss_310 .

Pavlović, R., Grujić, Marica, Dojnov, Biljana, Vujčić, Miroslava T., Nenadović, Vera, Ivanović, Jelisaveta, Vujčić, Zoran M., "Influence of nutrient substrates on the expression of cellulases in Cerambyx cerdo L. (Coleoptera: Cerambycidae) larvae" in Archives of Biological Sciences, 64, no. 2 (2012):757-765,
https://hdl.handle.net/21.15107/rcub_ibiss_310 .

TY  - JOUR
AU  - Dojnov, Biljana
AU  - Vujčić, Zoran M.
AU  - Bozić, Natasa M
AU  - Margetić, Aleksandra
AU  - Vujčić, Miroslava T.
AU  - Nenadović, Vera
AU  - Ivanović, Jelisaveta
PY  - 2012
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/1197
AB  - Captive breeding has been suggested as a method of conservation for many vertebrates, and is increasingly being proposed as a strategy for invertebrates. In this study, the growth, development and fertility of adults of the vulnerable cerambycid Morimus funereus reared in captivity are examined. Two oviposition cycles; from May to September and from January to March were studied and larvae from wild adults and from the progeny of captive adults (second generation larvae) were examined. Five to 12 instars were observed during larval development. Larval development was completed in 218 days (average) for the progeny of wild adults with an average mortality rate of 10.3% and in 226 days (average) for larvae from captive adults with mortality rate of 34.9%. First generation larval body weights were disparate during development, while second generation larvae had similar weights with no significant differences. In this study we have tested the potential of captive breaded M. funereus larvae as a model for investigation of digestive enzymes. Amylase from the midgut of larvae reared under laboratory conditions showed twofold higher specific activities with a decreased number of isoforms expressed, as compared to the enzyme from field-collected larvae. Captive breeding of M. funereus can be used in the future as a part of an effective conservation strategy for this rare insect species.
T2  - Journal of Insect Conservation
T1  - Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study
IS  - 2
VL  - 16
EP  - 247
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_1197
ER  - 

@article{
author = "Dojnov, Biljana and Vujčić, Zoran M. and Bozić, Natasa M and Margetić, Aleksandra and Vujčić, Miroslava T. and Nenadović, Vera and Ivanović, Jelisaveta",
year = "2012",
abstract = "Captive breeding has been suggested as a method of conservation for many vertebrates, and is increasingly being proposed as a strategy for invertebrates. In this study, the growth, development and fertility of adults of the vulnerable cerambycid Morimus funereus reared in captivity are examined. Two oviposition cycles; from May to September and from January to March were studied and larvae from wild adults and from the progeny of captive adults (second generation larvae) were examined. Five to 12 instars were observed during larval development. Larval development was completed in 218 days (average) for the progeny of wild adults with an average mortality rate of 10.3% and in 226 days (average) for larvae from captive adults with mortality rate of 34.9%. First generation larval body weights were disparate during development, while second generation larvae had similar weights with no significant differences. In this study we have tested the potential of captive breaded M. funereus larvae as a model for investigation of digestive enzymes. Amylase from the midgut of larvae reared under laboratory conditions showed twofold higher specific activities with a decreased number of isoforms expressed, as compared to the enzyme from field-collected larvae. Captive breeding of M. funereus can be used in the future as a part of an effective conservation strategy for this rare insect species.",
journal = "Journal of Insect Conservation",
title = "Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study",
number = "2",
volume = "16",
pages = "247",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_1197"
}

Dojnov, B., Vujčić, Z. M., Bozić, N. M., Margetić, A., Vujčić, M. T., Nenadović, V.,& Ivanović, J.. (2012). Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study. in Journal of Insect Conservation, 16(2).
https://hdl.handle.net/21.15107/rcub_ibiss_1197

Dojnov B, Vujčić ZM, Bozić NM, Margetić A, Vujčić MT, Nenadović V, Ivanović J. Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study. in Journal of Insect Conservation. 2012;16(2):null-247.
https://hdl.handle.net/21.15107/rcub_ibiss_1197 .

Dojnov, Biljana, Vujčić, Zoran M., Bozić, Natasa M, Margetić, Aleksandra, Vujčić, Miroslava T., Nenadović, Vera, Ivanović, Jelisaveta, "Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study" in Journal of Insect Conservation, 16, no. 2 (2012),
https://hdl.handle.net/21.15107/rcub_ibiss_1197 .

TY  - JOUR
AU  - Loncar, Nikola L
AU  - Vujčić, Zoran M.
AU  - Bozić, Natasa M
AU  - Ivanović, Jelisaveta
AU  - Nenadović, Vera
PY  - 2010
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/1354
AB  - Trypsin-like enzyme (TLE) from the anterior midgut of Morimus funereus larvae was purified by anion exchange chromatography and gel filtration chromatography and characterized. Specific TLE activity was increased 322-fold by purification of the crude midgut extract. The purified enzyme had a pH optimum of 9.0 (optimum pH range 8.5-9.5) and temperature optimum of 45 degrees C with the KM ratio of 0.065 mM for benzoyl-arginine-p-nitroanilide (BApNA). Among a number of inhibitors tested, the most efficient was benzamidine (K(I) value of 0.012 mM, Ic(50) value of 0.204 mM) while inhibition of TLE activity by SBTI, TLCK, and PMSF was partial. Almost all divalent cations tested enhanced the enzyme activity, amongst them Co(2+) and Mn(2+) stimulated TLE activity for 2.5 times. The purified TLE (after gel-filtration on Superose 12 column) had a molecular mass of 37.5 kDa with an isoelectric point over 9.3. Sodium dodecylsulphate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed one band of 38 kDa, suggesting that the enzyme is a monomer. (C) 2010 Wiley Periodicals, Inc.
T2  - Archives of Insect Biochemistry and Physiology
T1  - Purification and Properties of Trypsin-Like Enzyme From the Midgut of Morimus Funereus (Coleoptera, Cerambycidae) Larvae
IS  - 4
VL  - 74
EP  - 246
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_1354
ER  - 

@article{
author = "Loncar, Nikola L and Vujčić, Zoran M. and Bozić, Natasa M and Ivanović, Jelisaveta and Nenadović, Vera",
year = "2010",
abstract = "Trypsin-like enzyme (TLE) from the anterior midgut of Morimus funereus larvae was purified by anion exchange chromatography and gel filtration chromatography and characterized. Specific TLE activity was increased 322-fold by purification of the crude midgut extract. The purified enzyme had a pH optimum of 9.0 (optimum pH range 8.5-9.5) and temperature optimum of 45 degrees C with the KM ratio of 0.065 mM for benzoyl-arginine-p-nitroanilide (BApNA). Among a number of inhibitors tested, the most efficient was benzamidine (K(I) value of 0.012 mM, Ic(50) value of 0.204 mM) while inhibition of TLE activity by SBTI, TLCK, and PMSF was partial. Almost all divalent cations tested enhanced the enzyme activity, amongst them Co(2+) and Mn(2+) stimulated TLE activity for 2.5 times. The purified TLE (after gel-filtration on Superose 12 column) had a molecular mass of 37.5 kDa with an isoelectric point over 9.3. Sodium dodecylsulphate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed one band of 38 kDa, suggesting that the enzyme is a monomer. (C) 2010 Wiley Periodicals, Inc.",
journal = "Archives of Insect Biochemistry and Physiology",
title = "Purification and Properties of Trypsin-Like Enzyme From the Midgut of Morimus Funereus (Coleoptera, Cerambycidae) Larvae",
number = "4",
volume = "74",
pages = "246",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_1354"
}

Loncar, N. L., Vujčić, Z. M., Bozić, N. M., Ivanović, J.,& Nenadović, V.. (2010). Purification and Properties of Trypsin-Like Enzyme From the Midgut of Morimus Funereus (Coleoptera, Cerambycidae) Larvae. in Archives of Insect Biochemistry and Physiology, 74(4).
https://hdl.handle.net/21.15107/rcub_ibiss_1354

Loncar NL, Vujčić ZM, Bozić NM, Ivanović J, Nenadović V. Purification and Properties of Trypsin-Like Enzyme From the Midgut of Morimus Funereus (Coleoptera, Cerambycidae) Larvae. in Archives of Insect Biochemistry and Physiology. 2010;74(4):null-246.
https://hdl.handle.net/21.15107/rcub_ibiss_1354 .

Loncar, Nikola L, Vujčić, Zoran M., Bozić, Natasa M, Ivanović, Jelisaveta, Nenadović, Vera, "Purification and Properties of Trypsin-Like Enzyme From the Midgut of Morimus Funereus (Coleoptera, Cerambycidae) Larvae" in Archives of Insect Biochemistry and Physiology, 74, no. 4 (2010),
https://hdl.handle.net/21.15107/rcub_ibiss_1354 .

TY  - JOUR
AU  - Dojnov, Biljana
AU  - Lončar, N.
AU  - Božić, Nataša
AU  - Nenadović, Vera
AU  - Ivanović, Jelisaveta
AU  - Vujčić, Zoran M.
PY  - 2010
PY  - 2010
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/260
AB  - α-Amylase isoforms of Cerambyx cerdo larvae from the wild (ML and SL) and reared in the laboratory (ADL) were compared. Three amylase isoforms were presented in the SL and ML extracts while two isoforms were presented in the ADL according to zymogram after isoelectric focusing (IEF). All C. cerdo amylase isoforms were acidic proteins (pI < 3.5). Seven amylase isoforms (ACC 1-7) from the midgut of C. cerdo larvae were found in the ML midgut extract, six in the SL extract, and four in the ADL extract according to native PAGE zymogram. The ADL amylase had the highest activity. All crude midgut extracts of C. cerdo larvae were fractionated on a Superose 12 HR column. The molecular mass of the ACC was estimated to be 34 kDa.
AB  - Upoređene su izoforme α-amilaze larvi Cerambyx cerdo sakupljenih iz prirode (ML i SL) i gajenih na veštačkoj podlozi u laboratoriji (ADL). Zimogramskom detekcijom posle IEF-a po tri izoforme su detektovane u ML i SL ekstraktima, a u ADL dve izoforme. Sve amilazne izoforme iz C. cerdo su bile kisele (pI < 3.5). Zimogramskom detekcijom posle nativne elektroforeze sedam izoformi je detektovano u ML ekstraktu, šest u SL ekstraktu i četiri u ADL ekstraktu. Najveća amilazna aktivnost je detektovana u ADL ekstraktu. Svi ekstrakti srednjih creva larvi C. cerdo su frakcionisani na koloni Superose 12 HR. Molekulska masa ACC-a je bila 34 kDa.
T2  - Archives of Biological Sciences
T1  - Uporedna analiza izoformi α-amilaze iz srednjeg creva larvi Cerambyx cerdo L. (Coleoptera: Cerambycidae) iz prirode i gajenih na veštačkoj podlozi
T1  - Comparison of α-amylase isoforms from the midgut of Cerambyx cerdo L. (Coleoptera: Cerambycidae) larvae developed in the wild and on an artificial diet
IS  - 3
VL  - 62
SP  - 575
EP  - 584
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_260
ER  - 

@article{
author = "Dojnov, Biljana and Lončar, N. and Božić, Nataša and Nenadović, Vera and Ivanović, Jelisaveta and Vujčić, Zoran M.",
year = "2010, 2010",
abstract = "α-Amylase isoforms of Cerambyx cerdo larvae from the wild (ML and SL) and reared in the laboratory (ADL) were compared. Three amylase isoforms were presented in the SL and ML extracts while two isoforms were presented in the ADL according to zymogram after isoelectric focusing (IEF). All C. cerdo amylase isoforms were acidic proteins (pI < 3.5). Seven amylase isoforms (ACC 1-7) from the midgut of C. cerdo larvae were found in the ML midgut extract, six in the SL extract, and four in the ADL extract according to native PAGE zymogram. The ADL amylase had the highest activity. All crude midgut extracts of C. cerdo larvae were fractionated on a Superose 12 HR column. The molecular mass of the ACC was estimated to be 34 kDa., Upoređene su izoforme α-amilaze larvi Cerambyx cerdo sakupljenih iz prirode (ML i SL) i gajenih na veštačkoj podlozi u laboratoriji (ADL). Zimogramskom detekcijom posle IEF-a po tri izoforme su detektovane u ML i SL ekstraktima, a u ADL dve izoforme. Sve amilazne izoforme iz C. cerdo su bile kisele (pI < 3.5). Zimogramskom detekcijom posle nativne elektroforeze sedam izoformi je detektovano u ML ekstraktu, šest u SL ekstraktu i četiri u ADL ekstraktu. Najveća amilazna aktivnost je detektovana u ADL ekstraktu. Svi ekstrakti srednjih creva larvi C. cerdo su frakcionisani na koloni Superose 12 HR. Molekulska masa ACC-a je bila 34 kDa.",
journal = "Archives of Biological Sciences",
title = "Uporedna analiza izoformi α-amilaze iz srednjeg creva larvi Cerambyx cerdo L. (Coleoptera: Cerambycidae) iz prirode i gajenih na veštačkoj podlozi, Comparison of α-amylase isoforms from the midgut of Cerambyx cerdo L. (Coleoptera: Cerambycidae) larvae developed in the wild and on an artificial diet",
number = "3",
volume = "62",
pages = "575-584",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_260"
}

Dojnov, B., Lončar, N., Božić, N., Nenadović, V., Ivanović, J.,& Vujčić, Z. M.. (2010). Uporedna analiza izoformi α-amilaze iz srednjeg creva larvi Cerambyx cerdo L. (Coleoptera: Cerambycidae) iz prirode i gajenih na veštačkoj podlozi. in Archives of Biological Sciences, 62(3), 575-584.
https://hdl.handle.net/21.15107/rcub_ibiss_260

Dojnov B, Lončar N, Božić N, Nenadović V, Ivanović J, Vujčić ZM. Uporedna analiza izoformi α-amilaze iz srednjeg creva larvi Cerambyx cerdo L. (Coleoptera: Cerambycidae) iz prirode i gajenih na veštačkoj podlozi. in Archives of Biological Sciences. 2010;62(3):575-584.
https://hdl.handle.net/21.15107/rcub_ibiss_260 .

Dojnov, Biljana, Lončar, N., Božić, Nataša, Nenadović, Vera, Ivanović, Jelisaveta, Vujčić, Zoran M., "Uporedna analiza izoformi α-amilaze iz srednjeg creva larvi Cerambyx cerdo L. (Coleoptera: Cerambycidae) iz prirode i gajenih na veštačkoj podlozi" in Archives of Biological Sciences, 62, no. 3 (2010):575-584,
https://hdl.handle.net/21.15107/rcub_ibiss_260 .

TY  - JOUR
AU  - Lončar, N.
AU  - Božić, Nataša
AU  - Nenadović, Vera
AU  - Ivanović, Jelisaveta
AU  - Vujčić, Zoran M.
PY  - 2009
PY  - 2009
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/238
AB  - The pH along the midgut of M. funereus larvae had different values, being acidic in the anterior section and basic in the middle and posterior sections. Elastase- and chymotrypsin-like activities were highest in the middle, low in the anterior, and negligible in the posterior section of the midgut. Trypsin-like activities were detected along the whole midgut, with more than 90% of activity in the anterior section. The level of elastase- and chymotrypsin-like activity was very low compared to trypsin-like activity. In the anterior section of the midgut, two isoforms of trypsin-like enzymes were found, both being basic and almost completely inhibited by benzamidine.
AB  - pH vrednost duž srednjeg creva larvi M. funereus se razlikuje, kisela je u regionu prednjeg dela, dok je u srednjem i zadnjem delu bazna. Elastazama i himotripsinima slična aktivnost je najveća u srednjem delu srednjeg creva dok je u prednjem delu detektovana mala vrednost, a u zadnjem delu zanemarljiva. Tripsinima slična aktivnost je detektovana duž celog srednjeg creva, s tim da se više od 90 % aktivnosti detektuje u prednjem delu srednjeg creva. Zastupljenost elastazama i himotripsinima sličnih endopeptidaza je zanemarljivo mala u poređenju sa zastupljenošću tripsinima sličnih enzima. U prednjem delu srednjeg creva nalaze se dve izoforme tripsinima sličnih enzima, sa baznim pI vrednostima, koje su skoro u potpunosti inhibirane benzamidinom.
T2  - Archives of Biological Sciences
T1  - Karakterizacija tripsinima-sličnih enzima srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae)
T1  - Characterization of trypsin-like enzymes from the midgut of Morimus funereus (Coleoptera: Cerambycidae) larvae
IS  - 4
VL  - 61
SP  - 713
EP  - 718
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_238
ER  - 

@article{
author = "Lončar, N. and Božić, Nataša and Nenadović, Vera and Ivanović, Jelisaveta and Vujčić, Zoran M.",
year = "2009, 2009",
abstract = "The pH along the midgut of M. funereus larvae had different values, being acidic in the anterior section and basic in the middle and posterior sections. Elastase- and chymotrypsin-like activities were highest in the middle, low in the anterior, and negligible in the posterior section of the midgut. Trypsin-like activities were detected along the whole midgut, with more than 90% of activity in the anterior section. The level of elastase- and chymotrypsin-like activity was very low compared to trypsin-like activity. In the anterior section of the midgut, two isoforms of trypsin-like enzymes were found, both being basic and almost completely inhibited by benzamidine., pH vrednost duž srednjeg creva larvi M. funereus se razlikuje, kisela je u regionu prednjeg dela, dok je u srednjem i zadnjem delu bazna. Elastazama i himotripsinima slična aktivnost je najveća u srednjem delu srednjeg creva dok je u prednjem delu detektovana mala vrednost, a u zadnjem delu zanemarljiva. Tripsinima slična aktivnost je detektovana duž celog srednjeg creva, s tim da se više od 90 % aktivnosti detektuje u prednjem delu srednjeg creva. Zastupljenost elastazama i himotripsinima sličnih endopeptidaza je zanemarljivo mala u poređenju sa zastupljenošću tripsinima sličnih enzima. U prednjem delu srednjeg creva nalaze se dve izoforme tripsinima sličnih enzima, sa baznim pI vrednostima, koje su skoro u potpunosti inhibirane benzamidinom.",
journal = "Archives of Biological Sciences",
title = "Karakterizacija tripsinima-sličnih enzima srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae), Characterization of trypsin-like enzymes from the midgut of Morimus funereus (Coleoptera: Cerambycidae) larvae",
number = "4",
volume = "61",
pages = "713-718",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_238"
}

Lončar, N., Božić, N., Nenadović, V., Ivanović, J.,& Vujčić, Z. M.. (2009). Karakterizacija tripsinima-sličnih enzima srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae). in Archives of Biological Sciences, 61(4), 713-718.
https://hdl.handle.net/21.15107/rcub_ibiss_238

Lončar N, Božić N, Nenadović V, Ivanović J, Vujčić ZM. Karakterizacija tripsinima-sličnih enzima srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae). in Archives of Biological Sciences. 2009;61(4):713-718.
https://hdl.handle.net/21.15107/rcub_ibiss_238 .

Lončar, N., Božić, Nataša, Nenadović, Vera, Ivanović, Jelisaveta, Vujčić, Zoran M., "Karakterizacija tripsinima-sličnih enzima srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae)" in Archives of Biological Sciences, 61, no. 4 (2009):713-718,
https://hdl.handle.net/21.15107/rcub_ibiss_238 .

TY  - JOUR
AU  - Bozić, Natasa M
AU  - Ivanović, Jelisaveta
AU  - Bergstroem, Joergen
AU  - Nenadović, Vera
AU  - Larsson, Thomas
AU  - Vujčić, Zoran M.
PY  - 2008
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/1542
AB  - The major leucyl aminopeptidase (LAP) from the midgut of Morimus funereus larvae was purified and characterised. Specific LAP activity was increased 292-fold by purification of the crude midgut extract. The purified enzyme had a pH optimum of 7.5 (optimum pH range 7.0-8.5) and preferentially hydrolysed p-nitroanilides containing hydrophobic amino acids in the active site, with the highest V-max /K-M ratio for leucine-p-nitroanilide (LpNA). Among a number of inhibitors tested, the most efficient were 1, 10-phenanthroline having a K-i value of 0.12 mM and cysteine with K-i value of 0.31 mM, while EGTA stimulated LAP activity. Zn2+, Mg2+ and Mn2+ all showed bi-modal effects on LAP activity (activated at low concentrations and inhibited at high concentrations). The purified LAP (after gel filtration on Superose 6 column) had molecular mass of 400 kDa with an isoelectric point of 6.2. Sodium dodecylsulphate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed one band of 67 kDa, suggesting that the enzyme is a hexamer. Six peptide sequences from protein band were obtained using ESI/MS-MS analysis. Comparison of the obtained peptide sequences with the EMBL-EBI sequence analysis toolbox and the BLASTP database showed a high degree of identity with other insect aminopeptidases. (C) 2007 Elsevier Inc. All rights reserved.
T2  - Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology
T1  - Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae
IS  - 3
VL  - 149
EP  - 462
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_1542
ER  - 

@article{
author = "Bozić, Natasa M and Ivanović, Jelisaveta and Bergstroem, Joergen and Nenadović, Vera and Larsson, Thomas and Vujčić, Zoran M.",
year = "2008",
abstract = "The major leucyl aminopeptidase (LAP) from the midgut of Morimus funereus larvae was purified and characterised. Specific LAP activity was increased 292-fold by purification of the crude midgut extract. The purified enzyme had a pH optimum of 7.5 (optimum pH range 7.0-8.5) and preferentially hydrolysed p-nitroanilides containing hydrophobic amino acids in the active site, with the highest V-max /K-M ratio for leucine-p-nitroanilide (LpNA). Among a number of inhibitors tested, the most efficient were 1, 10-phenanthroline having a K-i value of 0.12 mM and cysteine with K-i value of 0.31 mM, while EGTA stimulated LAP activity. Zn2+, Mg2+ and Mn2+ all showed bi-modal effects on LAP activity (activated at low concentrations and inhibited at high concentrations). The purified LAP (after gel filtration on Superose 6 column) had molecular mass of 400 kDa with an isoelectric point of 6.2. Sodium dodecylsulphate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed one band of 67 kDa, suggesting that the enzyme is a hexamer. Six peptide sequences from protein band were obtained using ESI/MS-MS analysis. Comparison of the obtained peptide sequences with the EMBL-EBI sequence analysis toolbox and the BLASTP database showed a high degree of identity with other insect aminopeptidases. (C) 2007 Elsevier Inc. All rights reserved.",
journal = "Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology",
title = "Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae",
number = "3",
volume = "149",
pages = "462",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_1542"
}

Bozić, N. M., Ivanović, J., Bergstroem, J., Nenadović, V., Larsson, T.,& Vujčić, Z. M.. (2008). Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae. in Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology, 149(3).
https://hdl.handle.net/21.15107/rcub_ibiss_1542

Bozić NM, Ivanović J, Bergstroem J, Nenadović V, Larsson T, Vujčić ZM. Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae. in Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology. 2008;149(3):null-462.
https://hdl.handle.net/21.15107/rcub_ibiss_1542 .

Bozić, Natasa M, Ivanović, Jelisaveta, Bergstroem, Joergen, Nenadović, Vera, Larsson, Thomas, Vujčić, Zoran M., "Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae" in Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology, 149, no. 3 (2008),
https://hdl.handle.net/21.15107/rcub_ibiss_1542 .

TY  - JOUR
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Milovanović, Aleksandra
AU  - Nenadović, Vera
AU  - Ivanović, Jelisaveta
AU  - Vujčić, Zoran M.
PY  - 2008
PY  - 2008
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/199
AB  - Application of specific chromogenic substrates, use of class-specific inhibitors, and zymogram analysis enabled us to identify several peptidase classes in extracts of the midgut of Morimus funereus larvae. Zymogram analysis with gelatin as a peptidase substrate and phenylmethylsulfonyl fluoride as an inhibitor showed that serine peptidases were the most abundant endopeptidases in the midgut of M. funereus larvae. By zymogram analysis with gelatin as a peptidase substrate and 1,10-phenanthroline as an inhibitor, metallopeptidases were also detected. Analyses of serine peptidases with specific chromogenic substrates revealed dominance of elastase-like peptidases in extracts of the midgut of M. funereus larvae, with less pronounced chymotrypsin- and trypsin-like activities.
AB  - Primenom specifičnih hromogenih supstrata, klasno-specifičnih inhibitora i zimogramske analize identifikovano je nekoliko klasa peptidaza u sirovom ekstraktu srednjeg creva larvi koleoptere Morimus funereus. Zimogramskom analizom sa želatinom kao supstratom i fenilmetilsulfonil-fluoridom kao inhibitorom utvrđeno je da su serin-peptidaze najzastupljenije peptidaze u ekstraktu srednjeg creva larvi M. funereus. Zimogramskom analizom sa želatinom kao supstratom i 1,10-fenantrolinom kaoinhibitorom takođe su detektovane metalopeptidaze. Analizom serin-peptidaza, upotrebom specifičnih hromogenih supstrata, dokazano je da su dominantni elastazi-slični enzimi u sirovom ekstraktu srednjeg creva larvi M. funereus, dok su himotripsinima- i tripsinima-slični enzimi manje zastupljeni.
T2  - Archives of Biological Sciences
T1  - Karakterizacija endopeptidaza srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae)
T1  - Characterization of endopeptidases from the midgut of Morimus funereus (Coleoptera: Cerambycidae) larvae
IS  - 3
VL  - 60
SP  - 403
EP  - 409
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_199
ER  - 

@article{
author = "Božić, Nataša and Dojnov, Biljana and Milovanović, Aleksandra and Nenadović, Vera and Ivanović, Jelisaveta and Vujčić, Zoran M.",
year = "2008, 2008",
abstract = "Application of specific chromogenic substrates, use of class-specific inhibitors, and zymogram analysis enabled us to identify several peptidase classes in extracts of the midgut of Morimus funereus larvae. Zymogram analysis with gelatin as a peptidase substrate and phenylmethylsulfonyl fluoride as an inhibitor showed that serine peptidases were the most abundant endopeptidases in the midgut of M. funereus larvae. By zymogram analysis with gelatin as a peptidase substrate and 1,10-phenanthroline as an inhibitor, metallopeptidases were also detected. Analyses of serine peptidases with specific chromogenic substrates revealed dominance of elastase-like peptidases in extracts of the midgut of M. funereus larvae, with less pronounced chymotrypsin- and trypsin-like activities., Primenom specifičnih hromogenih supstrata, klasno-specifičnih inhibitora i zimogramske analize identifikovano je nekoliko klasa peptidaza u sirovom ekstraktu srednjeg creva larvi koleoptere Morimus funereus. Zimogramskom analizom sa želatinom kao supstratom i fenilmetilsulfonil-fluoridom kao inhibitorom utvrđeno je da su serin-peptidaze najzastupljenije peptidaze u ekstraktu srednjeg creva larvi M. funereus. Zimogramskom analizom sa želatinom kao supstratom i 1,10-fenantrolinom kaoinhibitorom takođe su detektovane metalopeptidaze. Analizom serin-peptidaza, upotrebom specifičnih hromogenih supstrata, dokazano je da su dominantni elastazi-slični enzimi u sirovom ekstraktu srednjeg creva larvi M. funereus, dok su himotripsinima- i tripsinima-slični enzimi manje zastupljeni.",
journal = "Archives of Biological Sciences",
title = "Karakterizacija endopeptidaza srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae), Characterization of endopeptidases from the midgut of Morimus funereus (Coleoptera: Cerambycidae) larvae",
number = "3",
volume = "60",
pages = "403-409",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_199"
}

Božić, N., Dojnov, B., Milovanović, A., Nenadović, V., Ivanović, J.,& Vujčić, Z. M.. (2008). Karakterizacija endopeptidaza srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae). in Archives of Biological Sciences, 60(3), 403-409.
https://hdl.handle.net/21.15107/rcub_ibiss_199

Božić N, Dojnov B, Milovanović A, Nenadović V, Ivanović J, Vujčić ZM. Karakterizacija endopeptidaza srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae). in Archives of Biological Sciences. 2008;60(3):403-409.
https://hdl.handle.net/21.15107/rcub_ibiss_199 .

Božić, Nataša, Dojnov, Biljana, Milovanović, Aleksandra, Nenadović, Vera, Ivanović, Jelisaveta, Vujčić, Zoran M., "Karakterizacija endopeptidaza srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae)" in Archives of Biological Sciences, 60, no. 3 (2008):403-409,
https://hdl.handle.net/21.15107/rcub_ibiss_199 .

TY  - JOUR
AU  - Božić, Nataša M.
AU  - Vujčić, Zoran M.
AU  - Nenadović, Vera A.
AU  - Ivanović, J.
PY  - 2004
PY  - 2004
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/98
T2  - Archives of Biological Sciences
T1  - Isoforms of leucyl-aminopeptidase of Cerambyx cerdo (Coleoptera, Cerambycidae) larvae
IS  - 1-2
VL  - 56
SP  - 2
EP  - 3
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_98
ER  - 

@article{
author = "Božić, Nataša M. and Vujčić, Zoran M. and Nenadović, Vera A. and Ivanović, J.",
year = "2004, 2004",
journal = "Archives of Biological Sciences",
title = "Isoforms of leucyl-aminopeptidase of Cerambyx cerdo (Coleoptera, Cerambycidae) larvae",
number = "1-2",
volume = "56",
pages = "2-3",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_98"
}

Božić, N. M., Vujčić, Z. M., Nenadović, V. A.,& Ivanović, J.. (2004). Isoforms of leucyl-aminopeptidase of Cerambyx cerdo (Coleoptera, Cerambycidae) larvae. in Archives of Biological Sciences, 56(1-2), 2-3.
https://hdl.handle.net/21.15107/rcub_ibiss_98

Božić NM, Vujčić ZM, Nenadović VA, Ivanović J. Isoforms of leucyl-aminopeptidase of Cerambyx cerdo (Coleoptera, Cerambycidae) larvae. in Archives of Biological Sciences. 2004;56(1-2):2-3.
https://hdl.handle.net/21.15107/rcub_ibiss_98 .

Božić, Nataša M., Vujčić, Zoran M., Nenadović, Vera A., Ivanović, J., "Isoforms of leucyl-aminopeptidase of Cerambyx cerdo (Coleoptera, Cerambycidae) larvae" in Archives of Biological Sciences, 56, no. 1-2 (2004):2-3,
https://hdl.handle.net/21.15107/rcub_ibiss_98 .

TY  - JOUR
AU  - Radotić, Ksenija
AU  - Dučić, Tanja M.
AU  - Prodanović, Radivoje M.
AU  - Vujčić, Zoran M.
AU  - Karadžić, Branko
AU  - Antić-Jovanović, Svetlana
PY  - 2003
PY  - 2003
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/27
AB  - We studied the soluble peroxidase and superoxid-dismutase activity peroxidase isoenzyme pattern and metal content in the needles of 2-year-old spruce grown on soils supplemented with cadmium and nickel concentrations from 3 to 30 mg kg -1 and 50 to 500 mg kg -1 respectively. The two metals were applied both separately and simultaneously. The kinetics of metal assimilation and total accumulated quantity depended on the type of treatment. Following metal exposure, an increase in peroxidase activity in the seedlings treated with Cd and Ni/Cd, and in superoxide-dismutase activity during Ni/Cd treatment was observed. A parallel change of peroxidase isoenzyme pattern occurred. There was a good correlation between accumulated metals in needles and enzyme activities. The effect of Cd on the measured parameters was shown to be stronger comparing to the effect of Ni. The results obtained show that peroxidase and superoxide-dismutase activity and peroxidase isoenzyme pattern could be used to evaluate the capacity of one part of the defense system in spruce seedlings to with-stand metal stress.
AB  - Proučavana je aktivnost slobodnih peroksidaza i superoksid-dismutaza izoenzimski profil peroksidaza i sadržaj metala u četinama dvogodišnjih smrča gajenih na zemljištu u koje su dodavani kadmijum i nikl u koncentracijama 3 do 30 mg kg -1 i 50 do 500 mg kg -1 respektivno. Metali su dodavani na dva načina: zasebno i istovremeno. Kinetika usvajanja metala i ukupna akumulirana količina zavisili su od vrste tretmana. U tretiranim izdancima došlo je do povećanja peroksidazne aktivnosti u slučaju tretmana kadmijumom i nikl/kadmijumom, kao i superoksid-dismutazne aktivnosti u toku tretmana nikl/kadmijumom, u odnosu na netretirane biljke. Istovremeno je došlo do promene izoenzimskog sastava peroksidaza. Koncentracija akumuliranih metala u četinama je bila u dobroj korelaciji sa enzimskim aktivnostima. Pokazano je da je uticaj kadmijuma na merene parametre jači u poređenju sa uticajem nikla. Dobijeni rezultati pokazuju da peroksidazna i superoksid-dismutazna aktivnost i izoenzimski profil peroksidaza mogu da se koriste za procenu kapaciteta jednog dela zaštitnog sistema u izdancima smrče u odnosu na stres izazvan metalima.
T2  - Jugoslovenska medicinska biohemija
T1  - Toksičnost nikla i kadmijuma u četinama smrče: uticaj zasebnih i kombinovanih tretmana na peroksidaznu i superoksid-dismutaznu aktivnost
T1  - Toxicity of nickel and cadmium in spruce seedlings: Effect of separated and combined treatments on peroxidase and superoxide-dismutase activity
IS  - 1
VL  - 22
SP  - 41
EP  - 52
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_27
ER  - 

@article{
author = "Radotić, Ksenija and Dučić, Tanja M. and Prodanović, Radivoje M. and Vujčić, Zoran M. and Karadžić, Branko and Antić-Jovanović, Svetlana",
year = "2003, 2003",
abstract = "We studied the soluble peroxidase and superoxid-dismutase activity peroxidase isoenzyme pattern and metal content in the needles of 2-year-old spruce grown on soils supplemented with cadmium and nickel concentrations from 3 to 30 mg kg -1 and 50 to 500 mg kg -1 respectively. The two metals were applied both separately and simultaneously. The kinetics of metal assimilation and total accumulated quantity depended on the type of treatment. Following metal exposure, an increase in peroxidase activity in the seedlings treated with Cd and Ni/Cd, and in superoxide-dismutase activity during Ni/Cd treatment was observed. A parallel change of peroxidase isoenzyme pattern occurred. There was a good correlation between accumulated metals in needles and enzyme activities. The effect of Cd on the measured parameters was shown to be stronger comparing to the effect of Ni. The results obtained show that peroxidase and superoxide-dismutase activity and peroxidase isoenzyme pattern could be used to evaluate the capacity of one part of the defense system in spruce seedlings to with-stand metal stress., Proučavana je aktivnost slobodnih peroksidaza i superoksid-dismutaza izoenzimski profil peroksidaza i sadržaj metala u četinama dvogodišnjih smrča gajenih na zemljištu u koje su dodavani kadmijum i nikl u koncentracijama 3 do 30 mg kg -1 i 50 do 500 mg kg -1 respektivno. Metali su dodavani na dva načina: zasebno i istovremeno. Kinetika usvajanja metala i ukupna akumulirana količina zavisili su od vrste tretmana. U tretiranim izdancima došlo je do povećanja peroksidazne aktivnosti u slučaju tretmana kadmijumom i nikl/kadmijumom, kao i superoksid-dismutazne aktivnosti u toku tretmana nikl/kadmijumom, u odnosu na netretirane biljke. Istovremeno je došlo do promene izoenzimskog sastava peroksidaza. Koncentracija akumuliranih metala u četinama je bila u dobroj korelaciji sa enzimskim aktivnostima. Pokazano je da je uticaj kadmijuma na merene parametre jači u poređenju sa uticajem nikla. Dobijeni rezultati pokazuju da peroksidazna i superoksid-dismutazna aktivnost i izoenzimski profil peroksidaza mogu da se koriste za procenu kapaciteta jednog dela zaštitnog sistema u izdancima smrče u odnosu na stres izazvan metalima.",
journal = "Jugoslovenska medicinska biohemija",
title = "Toksičnost nikla i kadmijuma u četinama smrče: uticaj zasebnih i kombinovanih tretmana na peroksidaznu i superoksid-dismutaznu aktivnost, Toxicity of nickel and cadmium in spruce seedlings: Effect of separated and combined treatments on peroxidase and superoxide-dismutase activity",
number = "1",
volume = "22",
pages = "41-52",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_27"
}

Radotić, K., Dučić, T. M., Prodanović, R. M., Vujčić, Z. M., Karadžić, B.,& Antić-Jovanović, S.. (2003). Toksičnost nikla i kadmijuma u četinama smrče: uticaj zasebnih i kombinovanih tretmana na peroksidaznu i superoksid-dismutaznu aktivnost. in Jugoslovenska medicinska biohemija, 22(1), 41-52.
https://hdl.handle.net/21.15107/rcub_ibiss_27

Radotić K, Dučić TM, Prodanović RM, Vujčić ZM, Karadžić B, Antić-Jovanović S. Toksičnost nikla i kadmijuma u četinama smrče: uticaj zasebnih i kombinovanih tretmana na peroksidaznu i superoksid-dismutaznu aktivnost. in Jugoslovenska medicinska biohemija. 2003;22(1):41-52.
https://hdl.handle.net/21.15107/rcub_ibiss_27 .

Radotić, Ksenija, Dučić, Tanja M., Prodanović, Radivoje M., Vujčić, Zoran M., Karadžić, Branko, Antić-Jovanović, Svetlana, "Toksičnost nikla i kadmijuma u četinama smrče: uticaj zasebnih i kombinovanih tretmana na peroksidaznu i superoksid-dismutaznu aktivnost" in Jugoslovenska medicinska biohemija, 22, no. 1 (2003):41-52,
https://hdl.handle.net/21.15107/rcub_ibiss_27 .

TY  - JOUR
AU  - Božić, Nataša M.
AU  - Vujčić, Zoran M.
AU  - Mrdaković, Marija
AU  - Ivanović, J.
AU  - Nenadović, Vera A.
PY  - 2001
PY  - 2001
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/382
AB  - Total proteolytic and leucyl-aminopeptidase activities were analyzed in the midgut of Cerambyx cerdo larvae fed on three different diets. The highest activities were found in the larvae fed on artificial diet.
AB  - U srednjem crevu larvi Cerambyx cerdo hranjenih sa tri različita supstrata analizirana je ukupna proteolitička i leucil-aminopeptidazna aktivnost. Najveća aktivnost nađena je kod larvi hranjenih veštačkim supstratom.
T2  - Acta entomologica Serbica
T1  - Proteinazne aktivnosti larvi ceramcerambyx cerdo (coleoptera, cerambycidae) hranjenih različitim supstratima
T1  - Midgut proteinase activities of cerambyx cerdo (coleoptera, cerambycidae) larvae fed on different diets
IS  - 1-2
VL  - 6
SP  - 147
EP  - 150
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_382
ER  - 

@article{
author = "Božić, Nataša M. and Vujčić, Zoran M. and Mrdaković, Marija and Ivanović, J. and Nenadović, Vera A.",
year = "2001, 2001",
abstract = "Total proteolytic and leucyl-aminopeptidase activities were analyzed in the midgut of Cerambyx cerdo larvae fed on three different diets. The highest activities were found in the larvae fed on artificial diet., U srednjem crevu larvi Cerambyx cerdo hranjenih sa tri različita supstrata analizirana je ukupna proteolitička i leucil-aminopeptidazna aktivnost. Najveća aktivnost nađena je kod larvi hranjenih veštačkim supstratom.",
journal = "Acta entomologica Serbica",
title = "Proteinazne aktivnosti larvi ceramcerambyx cerdo (coleoptera, cerambycidae) hranjenih različitim supstratima, Midgut proteinase activities of cerambyx cerdo (coleoptera, cerambycidae) larvae fed on different diets",
number = "1-2",
volume = "6",
pages = "147-150",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_382"
}

Božić, N. M., Vujčić, Z. M., Mrdaković, M., Ivanović, J.,& Nenadović, V. A.. (2001). Proteinazne aktivnosti larvi ceramcerambyx cerdo (coleoptera, cerambycidae) hranjenih različitim supstratima. in Acta entomologica Serbica, 6(1-2), 147-150.
https://hdl.handle.net/21.15107/rcub_ibiss_382

Božić NM, Vujčić ZM, Mrdaković M, Ivanović J, Nenadović VA. Proteinazne aktivnosti larvi ceramcerambyx cerdo (coleoptera, cerambycidae) hranjenih različitim supstratima. in Acta entomologica Serbica. 2001;6(1-2):147-150.
https://hdl.handle.net/21.15107/rcub_ibiss_382 .

Božić, Nataša M., Vujčić, Zoran M., Mrdaković, Marija, Ivanović, J., Nenadović, Vera A., "Proteinazne aktivnosti larvi ceramcerambyx cerdo (coleoptera, cerambycidae) hranjenih različitim supstratima" in Acta entomologica Serbica, 6, no. 1-2 (2001):147-150,
https://hdl.handle.net/21.15107/rcub_ibiss_382 .

TY  - JOUR
AU  - Božić, Nataša M.
AU  - Vujčić, Zoran M.
AU  - Janković Tomanić, Milena
AU  - Ivanović, J.
AU  - Nenadović, Vera A.
PY  - 2001
PY  - 2001
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/381
AB  - Different proteolytic activities using natural and synthetic substrates were analyzed in the midgut of Cerambyx cerdo larvae. Significant leucyl-aminopeptidase and elastase-like activities, as well as some trypsin-like activities were detected.
AB  - Korišćenjem prirodnih i sintetičkih supstrata analizirane su različite proteolitičke aktivnosti u srednjem crevu larve Cerambyx cerdo. Detektovane su značajne aktivnosti leucil-aminopeptidaze i elastazi sličnih enzima, kao i slabija aktivnost tripsinu sličnih enzima.
T2  - Acta entomologica Serbica
T1  - Proteinazne aktivnosti srednjeg creva larve cerambyx cerdo (coleoptera, cerambycidae)
T1  - Midgut proteinase activities of cerambyx cerdo (coleoptera, cerambycidae) larvae
IS  - 1-2
VL  - 6
SP  - 143
EP  - 146
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_381
ER  - 

@article{
author = "Božić, Nataša M. and Vujčić, Zoran M. and Janković Tomanić, Milena and Ivanović, J. and Nenadović, Vera A.",
year = "2001, 2001",
abstract = "Different proteolytic activities using natural and synthetic substrates were analyzed in the midgut of Cerambyx cerdo larvae. Significant leucyl-aminopeptidase and elastase-like activities, as well as some trypsin-like activities were detected., Korišćenjem prirodnih i sintetičkih supstrata analizirane su različite proteolitičke aktivnosti u srednjem crevu larve Cerambyx cerdo. Detektovane su značajne aktivnosti leucil-aminopeptidaze i elastazi sličnih enzima, kao i slabija aktivnost tripsinu sličnih enzima.",
journal = "Acta entomologica Serbica",
title = "Proteinazne aktivnosti srednjeg creva larve cerambyx cerdo (coleoptera, cerambycidae), Midgut proteinase activities of cerambyx cerdo (coleoptera, cerambycidae) larvae",
number = "1-2",
volume = "6",
pages = "143-146",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_381"
}

Božić, N. M., Vujčić, Z. M., Janković Tomanić, M., Ivanović, J.,& Nenadović, V. A.. (2001). Proteinazne aktivnosti srednjeg creva larve cerambyx cerdo (coleoptera, cerambycidae). in Acta entomologica Serbica, 6(1-2), 143-146.
https://hdl.handle.net/21.15107/rcub_ibiss_381

Božić NM, Vujčić ZM, Janković Tomanić M, Ivanović J, Nenadović VA. Proteinazne aktivnosti srednjeg creva larve cerambyx cerdo (coleoptera, cerambycidae). in Acta entomologica Serbica. 2001;6(1-2):143-146.
https://hdl.handle.net/21.15107/rcub_ibiss_381 .

Božić, Nataša M., Vujčić, Zoran M., Janković Tomanić, Milena, Ivanović, J., Nenadović, Vera A., "Proteinazne aktivnosti srednjeg creva larve cerambyx cerdo (coleoptera, cerambycidae)" in Acta entomologica Serbica, 6, no. 1-2 (2001):143-146,
https://hdl.handle.net/21.15107/rcub_ibiss_381 .