Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/68254
DC FieldValueLanguage
dc.contributor.authorHsieh, S.K.en_US
dc.contributor.authorTzen, J.T.C.en_US
dc.contributor.authorWu, T.Y.en_US
dc.contributor.authorChen, Y.J.en_US
dc.contributor.authorYang, W.H.en_US
dc.contributor.authorHuang, C.F.en_US
dc.contributor.authorHsieh, F.C.en_US
dc.contributor.authorJinn, T.R.en_US
dc.date2011zh_TW
dc.date.accessioned2014-06-11T05:56:31Z-
dc.date.available2014-06-11T05:56:31Z-
dc.identifier.issn0916-8451zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/68254-
dc.description.abstractThe maturation of mastoparan B, the major toxin peptide in the venom of Vespa basalis, requires enzymatic cleavage of its prosequence presumably via sequential liberation of dipeptides. The putative processing enzyme, dipeptidyl peptidase IV, was expressed as a glycosylated His-tag fusion protein (rDPP-IV) via the baculovirus expression system. rDPP-IV purified by one-step nickel-affinity chromatography was verified by Western blot and LC-MS/MS analysis. The k(cat)/K-m of rDPP-IV was determined to be in the range of 10-500 mM(-1).S-1 for five synthetic substrates. The optimal temperature and pH for rDPP-IV were determined to be 50 degrees C and pH 9. Enzymatic activity of rDPP-IV was significantly reduced by 80 and 60% in the presence of sitagliptin and phenylmethylsulfonyl fluoride respectively.en_US
dc.language.isoen_USzh_TW
dc.relationBioscience Biotechnology and Biochemistryen_US
dc.relation.ispartofseriesBioscience Biotechnology and Biochemistry, Volume 75, Issue 12, Page(s) 2371-2375.en_US
dc.relation.urihttp://dx.doi.org/10.1271/bbb.110571en_US
dc.subjectdipeptidyl peptidase IVen_US
dc.subjectmastoparan Ben_US
dc.subjectprosequence processingen_US
dc.subjectsitagliptinen_US
dc.subjectVespa basalisen_US
dc.subjectmastoparan-ben_US
dc.subjectenzyme-activityen_US
dc.subjectvenomen_US
dc.subjectpurificationen_US
dc.subjectbindingen_US
dc.subjectcloningen_US
dc.subjectgeneen_US
dc.titleFunctional Expression and Characterization of Dipeptidyl Peptidase IV from the Black-Bellied Hornet Vespa basalis in Sf21 Insect Cellsen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1271/bbb.110571zh_TW
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