Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/50406
標題: Molecular cloning of the precursor polypeptide of mastoparan B and its putative processing enzyme, dipeptidyl peptidase IV, from the black-bellied hornet, Vespa basalis
作者: 曾志正
Lee, V.S.Y.
Tu, W.C.
Jinn, T.R.
Peng, C.C.
Lin, L.J.
Tzen, J.T.C.
關鍵字: dipeptidyl peptidase IV;mastoparan B;propeptide;venom toxin;Vespa;basalis;honeybee prepromelittin;crystal-structure;melittin;venom;aminopeptidase;membranes;mechanism;sequence;protein
Project: Insect Molecular Biology
期刊/報告no:: Insect Molecular Biology, Volume 16, Issue 2, Page(s) 231-237.
摘要: 
Mastoparan B, a cationic toxin, is the major peptide component in the venom of Vespa basalis. Molecular cloning of its cDNA fragment revealed that this toxin was initially synthesized as a precursor polypeptide, containing an N-terminal signal sequence, a prosequence, the mature toxin, and an appendix glycine at C-terminus. Sequence alignment between precursors of mastoparan B and melittin from honeybee venom showed a significant conservation in prosequence. Alternate positions existing in both prosequences were either proline or alanine known as the potential cleaving sites for dipeptidyl peptidase IV. Subsequently, a putative dipeptidyl peptidase IV cDNA fragment was cloned from Vespa basalis venom gland. The prosequence may possibly be removed via sequential liberation of dipeptides during the processing of mastoparan B.
URI: http://hdl.handle.net/11455/50406
ISSN: 0962-1075
DOI: 10.1111/j.1365-2583.2006.00718.x
Appears in Collections:生物科技學研究所

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