在大肠杆菌中产生的一种钙激活中性蛋白酶（CANP）内源性抑制剂的片段保留了抑制活性。

A fragment of an endogenous inhibitor produced in Escherichia coli for calcium-activated neutral protease (CANP) retains an inhibitory activity.

作者信息

Imajoh S, Kawasaki H, Emori Y, Ishiura S, Minami Y, Sugita H, Imahori K, Suzuki K

出版信息

FEBS Lett. 1987 May 11;215(2):274-8. doi: 10.1016/0014-5793(87)80161-8.

Abstract

A C-terminal fragment of an endogenous rabbit liver inhibitor for calcium-activated neutral protease (CANP) was produced in Escherichia coli and its inhibitory activity was examined after purification. The truncated inhibitor (373 amino acid residues), which contains two internal repeat structures, inhibits 2 mol CANP whereas the native liver inhibitor (639 residues), containing four internal repeat structures, inhibits 4 mol CANP. This supports the hypothesis that the repeating unit is the functional unit of inhibition. The results also indicate that post-translational modification of the inhibitor is not essential for inhibition.

摘要

一种用于钙激活中性蛋白酶（CANP）的内源性兔肝抑制剂的C末端片段在大肠杆菌中产生，并在纯化后检测其抑制活性。截短的抑制剂（373个氨基酸残基）含有两个内部重复结构，可抑制2摩尔CANP，而天然肝抑制剂（639个残基）含有四个内部重复结构，可抑制4摩尔CANP。这支持了重复单元是抑制功能单元的假说。结果还表明，抑制剂的翻译后修饰对于抑制并非必不可少。