Strydom D J
Biochim Biophys Acta. 1977 Apr 25;491(2):361-9. doi: 10.1016/0005-2795(77)90279-3.
The amino acid sequence of venom component Vi2, a protein of low toxicity from Dendroaspis polylepis polylepis venom was determined by automatic sequence analysis in combination with sequence studies on tryptic peptides. This protein, the most retarded fraction of this venom on a cation-exchange resin, is a homologue of bovine pancreatic trypsin inhibitor consisting of a single chain of 57 amino acid residues containing six half-cystine residues. The active site lysyl residue of bovine trypsin inhibitor is conserved in Vi2 although large differences are found in the rest of the molecule.
通过自动序列分析结合胰蛋白酶肽段的序列研究,确定了绿曼巴蛇(Dendroaspis polylepis polylepis)毒液中低毒性蛋白毒液成分Vi2的氨基酸序列。该蛋白是这种毒液在阳离子交换树脂上滞留时间最长的组分,是牛胰蛋白酶抑制剂的同源物,由一条含57个氨基酸残基的单链组成,其中有六个半胱氨酸残基。尽管在分子的其余部分存在很大差异,但牛胰蛋白酶抑制剂的活性位点赖氨酰残基在Vi2中是保守的。