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Partial purification and characterization of midgut leucyl aminopeptidase of Morimus funereus (Coleoptera : Cerambycidae) larvae
dc.creator | Božić, Nataša | |
dc.creator | Vujčić, Zoran | |
dc.creator | Nenadovic, V | |
dc.creator | Ivanovic, J | |
dc.date.accessioned | 2021-05-27T14:37:12Z | |
dc.date.available | 2021-05-27T14:37:12Z | |
dc.date.issued | 2003 | |
dc.identifier.issn | 1096-4959 | |
dc.identifier.uri | https://cer.ihtm.bg.ac.rs/handle/123456789/4671 | |
dc.description.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. | en |
dc.publisher | Oxford : Pergamon-Elsevier Science Ltd | |
dc.rights | restrictedAccess | |
dc.source | Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology | |
dc.subject | cerambycid beetle | en |
dc.subject | leucyl aminopeptidase | en |
dc.subject | midgut proteinases | en |
dc.subject | Morimus funereus | en |
dc.subject | protemase inhibitors | en |
dc.subject | synthetic substrate | en |
dc.subject | xylophagous larvae | en |
dc.subject | zymogram | en |
dc.title | Partial purification and characterization of midgut leucyl aminopeptidase of Morimus funereus (Coleoptera : Cerambycidae) larvae | en |
dc.type | article | |
dc.rights.license | ARR | |
dcterms.abstract | Божић, Наташа; Ивановиц, Ј; Вујчић, Зоран; Ненадовиц, В; | |
dc.citation.volume | 134 | |
dc.citation.issue | 2 | |
dc.citation.spage | 231 | |
dc.citation.epage | 241 | |
dc.citation.other | 134(2): 231-241 | |
dc.citation.rank | M21 | |
dc.identifier.pmid | 12568801 | |
dc.identifier.doi | 10.1016/S1096-4959(02)00257-9 | |
dc.identifier.scopus | 2-s2.0-0037307262 | |
dc.identifier.wos | 000181093800004 | |
dc.type.version | publishedVersion | en |