Partial purification and characterization of midgut leucyl aminopeptidase of Morimus funereus (Coleoptera : Cerambycidae) larvae
Само за регистроване кориснике
2003
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Exopeptidases of Morimus funereus larvae were partially purified and characterized. Specific leucyl aminopeptidase (LAP) activity was increased eight-fold by gel filtration of the crude midgut extract. The partially purified LAP had a molecular mass greater than 100 kDa with pH optima from 7.0-9.0 and no strict substrate specificity. M. funereus LAP preferentially hydrolyzed p-nitroanilides with hydrophobic amino acids in the active site, with a K. for leucine-p-nitroanilide of 0.21 mM. Zymogram analysis of an electropherogram obtained by native polyacrylamide gel electrophoresis revealed four enzymatically active proteinases using leucine-p-nitroanilide and methionine-p-nitroanilide as substrates and two enzymatically active proteinases using lysine-p-nitroanilide as a substrate. Although the optimal temperature of LAP activity was 40 T, the enzyme was active over a broad temperature range from 2 to 60 T. Among a number of inhibitors tested, heavy metals and 1,10-phenanthroline comple...tely inhibited the enzyme, while methanol, ethanol and EGTA stimulated somewhat LAP activity. (C) 2002 Elsevier Science Inc. All rights reserved.
Кључне речи:
cerambycid beetle / leucyl aminopeptidase / midgut proteinases / Morimus funereus / protemase inhibitors / synthetic substrate / xylophagous larvae / zymogramИзвор:
Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology, 2003, 134, 2, 231-241Издавач:
- Oxford : Pergamon-Elsevier Science Ltd
DOI: 10.1016/S1096-4959(02)00257-9
ISSN: 1096-4959
PubMed: 12568801
WoS: 000181093800004
Scopus: 2-s2.0-0037307262
Институција/група
IHTMTY - JOUR AU - Božić, Nataša AU - Vujčić, Zoran AU - Nenadovic, V AU - Ivanovic, J PY - 2003 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/4671 AB - Exopeptidases of Morimus funereus larvae were partially purified and characterized. Specific leucyl aminopeptidase (LAP) activity was increased eight-fold by gel filtration of the crude midgut extract. The partially purified LAP had a molecular mass greater than 100 kDa with pH optima from 7.0-9.0 and no strict substrate specificity. M. funereus LAP preferentially hydrolyzed p-nitroanilides with hydrophobic amino acids in the active site, with a K. for leucine-p-nitroanilide of 0.21 mM. Zymogram analysis of an electropherogram obtained by native polyacrylamide gel electrophoresis revealed four enzymatically active proteinases using leucine-p-nitroanilide and methionine-p-nitroanilide as substrates and two enzymatically active proteinases using lysine-p-nitroanilide as a substrate. Although the optimal temperature of LAP activity was 40 T, the enzyme was active over a broad temperature range from 2 to 60 T. Among a number of inhibitors tested, heavy metals and 1,10-phenanthroline completely inhibited the enzyme, while methanol, ethanol and EGTA stimulated somewhat LAP activity. (C) 2002 Elsevier Science Inc. All rights reserved. PB - Oxford : Pergamon-Elsevier Science Ltd T2 - Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology T1 - Partial purification and characterization of midgut leucyl aminopeptidase of Morimus funereus (Coleoptera : Cerambycidae) larvae VL - 134 IS - 2 SP - 231 EP - 241 DO - 10.1016/S1096-4959(02)00257-9 ER -
@article{ author = "Božić, Nataša and Vujčić, Zoran and Nenadovic, V and Ivanovic, J", year = "2003", abstract = "Exopeptidases of Morimus funereus larvae were partially purified and characterized. Specific leucyl aminopeptidase (LAP) activity was increased eight-fold by gel filtration of the crude midgut extract. The partially purified LAP had a molecular mass greater than 100 kDa with pH optima from 7.0-9.0 and no strict substrate specificity. M. funereus LAP preferentially hydrolyzed p-nitroanilides with hydrophobic amino acids in the active site, with a K. for leucine-p-nitroanilide of 0.21 mM. Zymogram analysis of an electropherogram obtained by native polyacrylamide gel electrophoresis revealed four enzymatically active proteinases using leucine-p-nitroanilide and methionine-p-nitroanilide as substrates and two enzymatically active proteinases using lysine-p-nitroanilide as a substrate. Although the optimal temperature of LAP activity was 40 T, the enzyme was active over a broad temperature range from 2 to 60 T. Among a number of inhibitors tested, heavy metals and 1,10-phenanthroline completely inhibited the enzyme, while methanol, ethanol and EGTA stimulated somewhat LAP activity. (C) 2002 Elsevier Science Inc. All rights reserved.", publisher = "Oxford : Pergamon-Elsevier Science Ltd", journal = "Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology", title = "Partial purification and characterization of midgut leucyl aminopeptidase of Morimus funereus (Coleoptera : Cerambycidae) larvae", volume = "134", number = "2", pages = "231-241", doi = "10.1016/S1096-4959(02)00257-9" }
Božić, N., Vujčić, Z., Nenadovic, V.,& Ivanovic, J.. (2003). Partial purification and characterization of midgut leucyl aminopeptidase of Morimus funereus (Coleoptera : Cerambycidae) larvae. in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology Oxford : Pergamon-Elsevier Science Ltd., 134(2), 231-241. https://doi.org/10.1016/S1096-4959(02)00257-9
Božić N, Vujčić Z, Nenadovic V, Ivanovic J. Partial purification and characterization of midgut leucyl aminopeptidase of Morimus funereus (Coleoptera : Cerambycidae) larvae. in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology. 2003;134(2):231-241. doi:10.1016/S1096-4959(02)00257-9 .
Božić, Nataša, Vujčić, Zoran, Nenadovic, V, Ivanovic, J, "Partial purification and characterization of midgut leucyl aminopeptidase of Morimus funereus (Coleoptera : Cerambycidae) larvae" in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology, 134, no. 2 (2003):231-241, https://doi.org/10.1016/S1096-4959(02)00257-9 . .