银环蛇毒液中一种碱性磷脂酶A2的完整氨基酸序列。
The complete amino-acid sequence of a basic phospholipase A2 in the venom of Bungarus fasciatus.
作者信息
Liu C S, Chang C S, Leu H L, Chen S W, Lo T B
机构信息
Institute of Biological Chemistry, Academia Sinica, National Taiwan University.
出版信息
Biol Chem Hoppe Seyler. 1988 Nov;369(11):1227-33. doi: 10.1515/bchm3.1988.369.2.1227.
A basic phospholipase A2 (PLA2) was isolated and purified from the venom of Bungarus fasciatus. Four kinds of enzymes, lysyl endopeptidase, endoproteinase Asp-N, endoproteinase Glu-C and trypsin, were employed to elucidate the complete primary structure by means of gas-phase sequencing. The amino-acid sequence reveals 118 amino-acid residues containing seven pairs of half-cystine. It has 78% and 61% structural identities with PLA2 from Bungarus multicinctus and Naja melanoleuca DE-II, respectively.
从银环蛇毒中分离并纯化出一种碱性磷脂酶A2（PLA2）。使用四种酶，即赖氨酰内肽酶、天冬氨酸蛋白酶Asp-N、谷氨酸蛋白酶Glu-C和胰蛋白酶，通过气相测序来阐明其完整的一级结构。氨基酸序列显示有118个氨基酸残基，包含七对半胱氨酸。它与多带银环蛇和黑曼巴蛇DE-II的PLA2分别具有78%和61%的结构同源性。
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