双链巴曲酶原的一级结构，一种从巴西矛头蝮蛇毒中纯化得到的血管性血友病因子调节剂。
Primary structure of two-chain botrocetin, a von Willebrand factor modulator purified from the venom of Bothrops jararaca.
作者信息
Usami Y, Fujimura Y, Suzuki M, Ozeki Y, Nishio K, Fukui H, Titani K
机构信息
Division of Biomedical Polymer Science, School of Medicine, Fujita Health University, Aichi, Japan.
出版信息
Proc Natl Acad Sci U S A. 1993 Feb 1;90(3):928-32. doi: 10.1073/pnas.90.3.928.
The complete amino acid sequence and location of the disulfide bonds of two-chain botrocetin, which promotes platelet agglutination in the presence of von Willebrand factor, from venom of the snake Bothrops jararaca are presented. Sequences of the alpha and beta subunits were determined by analysis of peptides generated by digestion of the S-pyridylethylated protein with Achromobacter protease I or alpha-chymotrypsin and by chemical cleavage with cyanogen bromide or 2-(2'-nitrophenylsulfenyl)-3-methyl-3-bromoindolenine. Two-chain botrocetin is a heterodimer composed of the alpha subunit (consisting of 133 amino acid residues) and the beta subunit (consisting of 125 amino acid residues) held together by a disulfide bond. Seven disulfide bonds link half-cystine residues 2 to 13, 30 to 128, and 103 to 120 of the alpha subunit; 2 to 13, 30 to 121, and 98 to 113 of the beta subunit; and 80 of the alpha subunit to 75 of the beta subunit. In terms of amino acid sequence and disulfide bond location, two-chain botrocetin is homologous to echinoidin (a sea urchin lectin) and other C-type (Ca(2+)-dependent) lectins.
本文给出了双链蛇毒促凝素的完整氨基酸序列及其二硫键的位置。双链蛇毒促凝素存在于矛头蝮蛇（Bothrops jararaca）毒液中，在血管性血友病因子存在的情况下可促进血小板凝集。α亚基和β亚基的序列通过对S-吡啶基乙基化蛋白用嗜无色杆菌蛋白酶I或α-胰凝乳蛋白酶消化产生的肽段进行分析，以及用溴化氰或2-(2'-硝基苯磺酰基)-3-甲基-3-溴吲哚进行化学裂解来确定。双链蛇毒促凝素是一种异二聚体，由α亚基（由133个氨基酸残基组成）和β亚基（由125个氨基酸残基组成）通过一个二硫键连接而成。七个二硫键将α亚基的半胱氨酸残基2与13、30与128以及103与120相连；将β亚基的半胱氨酸残基2与13、30与121以及98与113相连；并将α亚基的80位与β亚基的75位相连。就氨基酸序列和二硫键位置而言，双链蛇毒促凝素与海胆素（一种海胆凝集素）和其他C型（钙依赖性）凝集素同源。
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