Suppr超能文献

关于组织蛋白酶L的底物特异性

On the substrate specificity of cathepsin L.

作者信息

Kirschke H

出版信息

Acta Biol Med Ger. 1981;40(10-11):1427-31.

PMID:6282022
Abstract

A view is given on the maximal hydrolysis of proteins by cathepsin L (EC 3.4.22.15) in dependence on the pH. The overall degradation of several proteins at pH values lower than pH 6.0 implies a very broad specificity, whereas at pH 7.0 and 7.5 cathepsin L seems to act on proteins cleaving only restricted specific peptide bonds. Some kinetic constants are given for the three synthetic substrates of cathepsin L which are known so far: Bz-Arg-NH2, Z-Lys-OPhNO2 and Z-Phe-Arg-NMec. They cannot be used as completely specific substrates of cathepsin L, because all of them are hydrolysed by cathepsin B and also other proteinases.

摘要

给出了组织蛋白酶L(EC 3.4.22.15)对蛋白质的最大水解作用与pH的关系。在pH值低于6.0时几种蛋白质的整体降解表明其具有非常广泛的特异性,而在pH 7.0和7.5时,组织蛋白酶L似乎仅作用于切割有限特定肽键的蛋白质。给出了目前已知的组织蛋白酶L的三种合成底物的一些动力学常数:Bz-Arg-NH2、Z-Lys-OPhNO2和Z-Phe-Arg-NMec。它们不能用作组织蛋白酶L的完全特异性底物,因为所有这些底物都会被组织蛋白酶B和其他蛋白酶水解。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验