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The possibility of the double head of leguminous STI(Kunitz) family inhibitors.

豆科STI(Kunitz)家族抑制剂双头的可能性。

基本信息

批准号：
62580121
负责人：
HARA Saburo
金额：
$ 1.09万
依托单位：
Osaka University
依托单位国家：
日本
项目类别：
Grant-in-Aid for General Scientific Research (C)
财政年份：
1987
资助国家：
日本
起止时间：
1987 至 1988
项目状态：
已结题

项目摘要

1) The complete amino acid sequence of winged bean chymotrypsin inhibitor 3 (WCI-3) was determined by the conventional methods. WCI-3 consisted of 183 amino acid residues, but was heterogeneous in the carboxyl terminal region. The sequence of WCI-3 was highly homologous with those of STI(Kunitz) family inhibitors.2) WCI-3 was treated with porcine chymotrypsin at pH 3.0. Chymotrypsin, however, hydrolyzed only the first reactive site (Leu(65)-Ser(66)). Onthe trial to cleave the second reactive site oF WCI-3 using several chymotrypsin-family enzymes, elastase, subtilisin, SGPS and SGPB, no enzyme could cleave the peptide bond of the second reactive site. The similar studies were done using the soybean trypsin inhibitor (Kunitz) (STI) Ti^a. The results suggested that the second reactive site of Ti^a might be located at or near Met(84)-Leu(85).

1)用常规方法测定了四棱豆胰凝乳蛋白酶抑制剂3（WCI-3）的全氨基酸序列。WCI-3由183个氨基酸残基组成，但在羧基末端区域是异质的。WCI-3与STI（Kunitz）家族成员的序列高度同源。2）WCI-3在pH3.0的条件下用猪糜蛋白酶处理。然而，糜蛋白酶仅水解第一反应位点（Leu（65）-Ser（66））。在用几种胰凝乳蛋白酶家族的酶，弹性蛋白酶，枯草杆菌蛋白酶，SGPS和SGPB切割WCI-3的第二反应位点的试验中，没有一种酶能切割第二反应位点的肽键。使用大豆胰蛋白酶抑制剂（Kunitz）（STI）Ti^a进行类似的研究。结果表明，Ti^a的第二反应位点可能位于Met（84）-Leu（85）或其附近。