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|標題:||Functional Expression and Characterization of Dipeptidyl Peptidase IV from the Black-Bellied Hornet Vespa basalis in Sf21 Insect Cells||作者:||Hsieh, S.K.
|關鍵字:||dipeptidyl peptidase IV;mastoparan B;prosequence processing;sitagliptin;Vespa basalis;mastoparan-b;enzyme-activity;venom;purification;binding;cloning;gene||Project:||Bioscience Biotechnology and Biochemistry||期刊/報告no：:||Bioscience Biotechnology and Biochemistry, Volume 75, Issue 12, Page(s) 2371-2375.||摘要:||
The 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.
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