来自食鱼蝮（东部水腹蛇）的蛇毒凝集素（APL）的一级结构和生物学活性

Primary structure and biological activity of snake venom lectin (APL) from Agkistrodon p. piscivorus (Eastern cottonmouth).

作者信息

Komori Y, Nikai T, Tohkai T, Sugihara H

机构信息

Department of Microbiology, Faculty of Pharmacy, Meijo University, Nagoya, Japan.

出版信息

Toxicon. 1999 Jul;37(7):1053-64. doi: 10.1016/s0041-0101(98)00239-6.

DOI:10.1016/s0041-0101(98)00239-6

PMID:10484740

Abstract

A lectin (APL) was purified from the venom of Agkistrodon piscivorus piscivorus (Eastern cottonmouth moccasin). APL is a disulfide-linked, homodimeric protein consisting of identical monomers of molecular weight 16,200. Native rabbit and human erythrocytes were agglutinated by APL and the activity was found to be calcium-dependent. Galactose, lactose, rhamnose and EGTA strongly inhibited the hemagglutination activity of APL. The complete amino acid sequence determined by Edman sequencing of the S-pyridylethylated derivative and its peptides derived from enzymatic digestion indicate the structure of APL to be highly homologous with lectins and the platelet glycoprotein Ib (GPIb)-binding proteins isolated from other snake venoms. These results suggest that APL belongs to the C-type beta-galactoside binding lectin family which possess structural similarities with the C-terminal carbohydrate-recognition domain (CRD) of animal membrane lectins.

摘要

从食鱼蝮（东部水腹蛇）的毒液中纯化出一种凝集素（APL）。APL是一种通过二硫键连接的同二聚体蛋白，由分子量为16,200的相同单体组成。天然兔和人红细胞可被APL凝集，且该活性呈钙依赖性。半乳糖、乳糖、鼠李糖和乙二醇双四乙酸（EGTA）强烈抑制APL的血凝活性。通过对S-吡啶基乙基化衍生物及其酶切肽段进行埃德曼测序确定的完整氨基酸序列表明，APL的结构与从其他蛇毒中分离出的凝集素和血小板糖蛋白Ib（GPIb）结合蛋白高度同源。这些结果表明，APL属于C型β-半乳糖苷结合凝集素家族，该家族与动物膜凝集素的C端碳水化合物识别结构域（CRD）具有结构相似性。