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dc.creatorBožić, Nataša
dc.creatorIvanović, J.
dc.creatorNenadović, V.
dc.creatorBergström, J.
dc.creatorLarsson, T.
dc.creatorVujčić, Zoran
dc.date.accessioned2019-01-30T17:18:49Z
dc.date.available2019-01-30T17:18:49Z
dc.date.issued2008
dc.identifier.issn1096-4959
dc.identifier.urihttp://cer.ihtm.bg.ac.rs/handle/123456789/463
dc.description.abstractThe 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.en
dc.publisherElsevier Science Inc, New York
dc.relationinfo:eu-repo/grantAgreement/MESTD/MPN2006-2010/142026/RS//
dc.rightsrestrictedAccess
dc.sourceComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
dc.subjectCerambycid beetleen
dc.subjectIsoformen
dc.subjectLeucyl aminopeptidaseen
dc.subjectMidguten
dc.subjectMorimus funereusen
dc.subjectXylophagous larvaeen
dc.titlePurification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvaeen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractИвановић, Ј.; Божић, Наташа; Бергстрöм, Ј.; Вујчић, З.; Ларссон, Т.; Ненадовић, В.;
dc.citation.volume149
dc.citation.issue3
dc.citation.spage454
dc.citation.epage462
dc.citation.other149(3): 454-462
dc.citation.rankM22
dc.identifier.pmid18155948
dc.identifier.doi10.1016/j.cbpb.2007.11.006
dc.identifier.rcubConv_4133
dc.identifier.scopus2-s2.0-39049120322
dc.identifier.wos000253576300007
dc.type.versionpublishedVersion


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