来自链霉菌的类SSI蛋白酶抑制剂的分离与部分特性分析

Isolation and partial characterization of SSI-like protease inhibitors from Streptomyces.

作者信息

Taguchi S, Kojima S, Kumagai I, Ogawara H, Miura K, Momose H

机构信息

Department of Biological Science and Technology, Science University of Tokyo, Chiba, Japan.

出版信息

FEMS Microbiol Lett. 1992 Dec 1;78(2-3):293-7. doi: 10.1016/0378-1097(92)90043-n.

DOI:10.1016/0378-1097(92)90043-n

PMID:1490613

Abstract

We attempted to screen a series of Streptomyces subtilisin inhibitor-like (SIL) proteins among several Streptomyces strains by using a highly sensitive assay system established by us. Of six randomly tested strains, four were found to produce SIL inhibitors as their major secreted proteins, suggesting that they might be distributed in a high frequency among this genus. Three inhibitors exhibited inhibition of both subtilisin BPN' and trypsin. Comparison of the amino terminal sequences of these isolated proteins with those of other reported SIL inhibitors revealed that the beta 1- and beta 2-sheets in SSI were highly conserved.

摘要

我们试图通过使用我们建立的高灵敏度检测系统，在几种链霉菌菌株中筛选一系列枯草杆菌蛋白酶抑制剂样（SIL）蛋白。在随机测试的6个菌株中，发现有4个菌株产生SIL抑制剂作为其主要分泌蛋白，这表明它们可能在该属中高频分布。三种抑制剂对枯草杆菌蛋白酶BPN'和胰蛋白酶均有抑制作用。将这些分离蛋白的氨基末端序列与其他已报道的SIL抑制剂的序列进行比较，发现SSI中的β1和β2折叠高度保守。