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大豆胰蛋白酶抑制剂的研究。X. 四种大豆双头蛋白酶抑制剂的分离及部分特性鉴定

Studies on soybean trypsin inhibitors. X. Isolation and partial characterization of four soybean double-headed proteinase inhibitors.

作者信息

Odani S, Ikenaka T

出版信息

J Biochem. 1977 Dec;82(6):1513-22. doi: 10.1093/oxfordjournals.jbchem.a131845.

DOI:10.1093/oxfordjournals.jbchem.a131845
PMID:599140
Abstract

Four Bowman-Birk type double-headed inhibitors (B, C-II, D-II, and E-I) were isolated from soybeans. Inhibitor B was different from Bowman-Birk inhibitor only in chromatographic behavior. One mole of C-II inhibited one mole each of bovine trypsin and bovine alpha-chymotrypsin, probably at the same site, and porcine elastase at another reactive site. In the ordinary assay system D-II and E-I inhibited only trypsin activity at a non-stoichiometric inhibitor-enzyme ratio of 1:1.4, and the complexes had rather high dissociation constants. These inhibitors were all inactive toward subtilisin BPN'.

摘要

从大豆中分离出四种鲍曼-伯克型双头抑制剂（B、C-II、D-II和E-I）。抑制剂B与鲍曼-伯克抑制剂的区别仅在于色谱行为。1摩尔的C-II抑制1摩尔的牛胰蛋白酶和1摩尔的牛α-糜蛋白酶，可能作用于同一位点，而抑制猪弹性蛋白酶则作用于另一个反应位点。在常规测定系统中，D-II和E-I仅以1:1.4的非化学计量抑制剂-酶比例抑制胰蛋白酶活性，且复合物具有相当高的解离常数。这些抑制剂对枯草杆菌蛋白酶BPN'均无活性。

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