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弗氏链霉菌的蛋白酶。III. 角蛋白分解蛋白酶的催化及一些物理化学性质

Proteinases of Streptomyces fradiae. III. Catalytic and some physico- chemical properties of keratinolytic proteinase.

作者信息

Galas E, Kałuźewska M

机构信息

Institute of Technical Biochemistry, Technical University, Lódź, Poland.

出版信息

Acta Microbiol Pol. 1992;41(3-4):169-177.

PMID:1284846
Abstract

It has been shown that keratinase--proteinase PIV, the main enzyme of the proteolytic system of S. fradiae, is characterized by high effectiveness in its action on AcAla3OMe--exceeding elastase in catalytic effectiveness several times. This proteinase also cleaves ester and amide bonds formed by the residues of aromatic and basic amino acids, but with a lower effectiveness than chymotrypsin or trypsin. It has also been shown that proteinase IV is a typical serine enzyme highly sensitive to DFP, acting in strongly alkaline pH (about 11.2), with molecular weight 24 kDa and does not contain cysteine.

摘要

已表明,角蛋白酶——蛋白酶PIV,是弗氏链霉菌蛋白水解系统的主要酶,其对乙酰丙氨酸甲酯的作用具有高效性,催化效率比弹性蛋白酶高出数倍。这种蛋白酶还能切割由芳香族和碱性氨基酸残基形成的酯键和酰胺键,但其效率低于胰凝乳蛋白酶或胰蛋白酶。还表明,蛋白酶IV是一种典型的丝氨酸酶,对二异丙基氟磷酸酯高度敏感,在强碱性pH(约11.2)下发挥作用,分子量为24 kDa,且不含半胱氨酸。

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