TY  - JOUR
AU  - Božić, Nataša
AU  - Ivanović, J.
AU  - Nenadović, V.
AU  - Bergström, J.
AU  - Larsson, T.
AU  - Vujčić, Zoran
PY  - 2008
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/463
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 Vmax / KM ratio for leucine-p-nitroanilide (LpNA). Among a number of inhibitors tested, the most efficient were 1,10-phenanthroline having a Ki value of 0.12 mM and cysteine with Ki 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.
PB  - Elsevier Science Inc, New York
T2  - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
T1  - Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae
VL  - 149
IS  - 3
SP  - 454
EP  - 462
DO  - 10.1016/j.cbpb.2007.11.006
ER  - 

@article{
author = "Božić, Nataša and Ivanović, J. and Nenadović, V. and Bergström, J. and Larsson, T. and Vujčić, Zoran",
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 Vmax / KM ratio for leucine-p-nitroanilide (LpNA). Among a number of inhibitors tested, the most efficient were 1,10-phenanthroline having a Ki value of 0.12 mM and cysteine with Ki 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.",
publisher = "Elsevier Science Inc, New York",
journal = "Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology",
title = "Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae",
volume = "149",
number = "3",
pages = "454-462",
doi = "10.1016/j.cbpb.2007.11.006"
}

Božić, N., Ivanović, J., Nenadović, V., Bergström, J., Larsson, T.,& Vujčić, Z.. (2008). Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae. in Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Elsevier Science Inc, New York., 149(3), 454-462.
https://doi.org/10.1016/j.cbpb.2007.11.006

Božić N, Ivanović J, Nenadović V, Bergström J, Larsson T, Vujčić Z. Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae. in Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology. 2008;149(3):454-462.
doi:10.1016/j.cbpb.2007.11.006 .

Božić, Nataša, Ivanović, J., Nenadović, V., Bergström, J., Larsson, T., Vujčić, Zoran, "Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae" in Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, 149, no. 3 (2008):454-462,
https://doi.org/10.1016/j.cbpb.2007.11.006 . .

TY  - JOUR
AU  - Dojnov, Biljana
AU  - Božić, Nataša
AU  - Nenadović, V.
AU  - Ivanović, J.
AU  - Vujčić, Zoran
PY  - 2008
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/459
AB  - Using soluble starch as a substrate five isoforms of α-amylase were identified in a crude extract of Morimus funereus larvae. The main α-amylase (termed AMF-3) was purified by gel filtration chromatography and anion exchange chromatography to obtain a single band on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Its enzymatic purity was confirmed by an in-gel activity assay after SDS-PAGE. The purity of AMF-3 was increased 112-fold with a 15.4% yield. AMF-3 had apparent molecular masses of 33 and 31 kDa when analysed using SDS-PAGE and Superdex 75 FPLC gel filtration chromatography, respectively and a calculated isoelectric point of 3.2. Purified AMF-3 showed maximal activity at pH 5.2 and had an optimum activity temperature of 45 °C. AMF-3 retained over 90% of its maximum activity at temperatures from 45 to 60 °C. AMF-3 exhibited a high affinity towards soluble starch with a Km value of 0.43 mg/mL. Maximal AMF-3 activity was achieved in the presence of 0.1 mM CaCl2, while at higher concentrations its activity decreased. AMF-3 activity increased with increasing NaCl concentration. AMF-3 activity was significantly inhibited by α-amylase wheat inhibitor. Using a number of raw starch substrates maximum AMF-3 activity was achieved with horse-radish starch, in contrast to undetectable activity towards potato starch.
PB  - Elsevier Science Inc, New York
T2  - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
T1  - Purification and properties of midgut α-amylase isolated from Morimus funereus (Coleoptera: Cerambycidae) larvae
VL  - 149
IS  - 1
SP  - 153
EP  - 160
DO  - 10.1016/j.cbpb.2007.09.009
ER  - 

@article{
author = "Dojnov, Biljana and Božić, Nataša and Nenadović, V. and Ivanović, J. and Vujčić, Zoran",
year = "2008",
abstract = "Using soluble starch as a substrate five isoforms of α-amylase were identified in a crude extract of Morimus funereus larvae. The main α-amylase (termed AMF-3) was purified by gel filtration chromatography and anion exchange chromatography to obtain a single band on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Its enzymatic purity was confirmed by an in-gel activity assay after SDS-PAGE. The purity of AMF-3 was increased 112-fold with a 15.4% yield. AMF-3 had apparent molecular masses of 33 and 31 kDa when analysed using SDS-PAGE and Superdex 75 FPLC gel filtration chromatography, respectively and a calculated isoelectric point of 3.2. Purified AMF-3 showed maximal activity at pH 5.2 and had an optimum activity temperature of 45 °C. AMF-3 retained over 90% of its maximum activity at temperatures from 45 to 60 °C. AMF-3 exhibited a high affinity towards soluble starch with a Km value of 0.43 mg/mL. Maximal AMF-3 activity was achieved in the presence of 0.1 mM CaCl2, while at higher concentrations its activity decreased. AMF-3 activity increased with increasing NaCl concentration. AMF-3 activity was significantly inhibited by α-amylase wheat inhibitor. Using a number of raw starch substrates maximum AMF-3 activity was achieved with horse-radish starch, in contrast to undetectable activity towards potato starch.",
publisher = "Elsevier Science Inc, New York",
journal = "Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology",
title = "Purification and properties of midgut α-amylase isolated from Morimus funereus (Coleoptera: Cerambycidae) larvae",
volume = "149",
number = "1",
pages = "153-160",
doi = "10.1016/j.cbpb.2007.09.009"
}

Dojnov, B., Božić, N., Nenadović, V., Ivanović, J.,& Vujčić, Z.. (2008). Purification and properties of midgut α-amylase isolated from Morimus funereus (Coleoptera: Cerambycidae) larvae. in Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Elsevier Science Inc, New York., 149(1), 153-160.
https://doi.org/10.1016/j.cbpb.2007.09.009

Dojnov B, Božić N, Nenadović V, Ivanović J, Vujčić Z. Purification and properties of midgut α-amylase isolated from Morimus funereus (Coleoptera: Cerambycidae) larvae. in Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology. 2008;149(1):153-160.
doi:10.1016/j.cbpb.2007.09.009 .

Dojnov, Biljana, Božić, Nataša, Nenadović, V., Ivanović, J., Vujčić, Zoran, "Purification and properties of midgut α-amylase isolated from Morimus funereus (Coleoptera: Cerambycidae) larvae" in Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, 149, no. 1 (2008):153-160,
https://doi.org/10.1016/j.cbpb.2007.09.009 . .

TY  - JOUR
AU  - Božić, Nataša
AU  - Vujčić, Zoran
AU  - Nenadović, Vera A.
AU  - Ivanović, J.
PY  - 2004
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/158
PB  - University of Belgrade, University of Novi Sad
T2  - Archives of Biological Sciences
T1  - Isoforms of leucyl-aminopeptidase of Cerambyx cerdo (Coleoptera, Cerambycidae) larvae
VL  - 56
IS  - 1-2
SP  - 2
EP  - 3
DO  - 10.2298/ABS0402021B
ER  - 

@article{
author = "Božić, Nataša and Vujčić, Zoran and Nenadović, Vera A. and Ivanović, J.",
year = "2004",
publisher = "University of Belgrade, University of Novi Sad",
journal = "Archives of Biological Sciences",
title = "Isoforms of leucyl-aminopeptidase of Cerambyx cerdo (Coleoptera, Cerambycidae) larvae",
volume = "56",
number = "1-2",
pages = "2-3",
doi = "10.2298/ABS0402021B"
}

Božić, N., Vujčić, Z., Nenadović, V. A.,& Ivanović, J.. (2004). Isoforms of leucyl-aminopeptidase of Cerambyx cerdo (Coleoptera, Cerambycidae) larvae. in Archives of Biological Sciences
University of Belgrade, University of Novi Sad., 56(1-2), 2-3.
https://doi.org/10.2298/ABS0402021B

Božić N, Vujčić Z, 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.
doi:10.2298/ABS0402021B .

Božić, Nataša, Vujčić, Zoran, 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://doi.org/10.2298/ABS0402021B . .