Identification and molecular cloning of novel trypsin inhibitor analogs from the dermal venom of the Oriental fire-bellied toad (Bombina orientalis) and the European yellow-bellied toad (Bombina variegata)

被引:25
作者
Chen, TB [1 ]
Shaw, C [1 ]
机构
[1] Univ Ulster, Sch Biomed Sci, Pharmaceut Biotechnol Res Grp, Coleraine BT52 1SA, Londonderry, North Ireland
关键词
amphibian; mass spectrometry; trypsin inhibitor; cDNA cloning;
D O I
10.1016/S0196-9781(03)00165-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The structural diversity of polypeptides in amphibian skin secretion probably reflects different roles in dermal regulation or in defense against predators. Here we report the structures of two novel trypsin inhibitor analogs, BOTI and BVTI, from the dermal venom of the toads, Bombina orientalis and Bombina variegata. Cloning of their respective precursors was achieved from lyophilized venom cDNA libraries for the first time. Amino acid alignment revealed that both deduced peptides, consisting of 60 amino acid residues, including 10 cysteines and the reactive center motif, -CDKKC-, can be affirmed as structural homologs of the trypsin inhibitor from Bombina bombina skin. (C) 2003 Elsevier Inc. All rights reserved.
引用
收藏
页码:873 / 880
页数:8
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