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A型产气荚膜梭菌孢子溶菌酶的纯化及性质

Purification and properties of spore-lytic enzymes from Clostridium perfringens type A spores.

作者信息

Gombas D E, Labbe R G

出版信息

J Gen Microbiol. 1985 Jun;131(6):1487-96. doi: 10.1099/00221287-131-6-1487.

Abstract

Spores of Clostridium perfringens contain at least two spore-lytic enzymes active in hydrolysing cortical peptidoglycan. One enzyme has been purified 1800-fold and has a molecular weight of 17 400 determined from chromatography on Sephadex G-75. Two protein bands were apparent after SDS-PAGE. The isolated enzyme was investigated for response to temperature, pH, ionic strength and enzyme inhibitors, and for mode of action. A second enzyme activity, differing from the first in apparent molecular weight (29 800) as determined by gel exclusion chromatography, and also in its pH optimum and activity on cortical substrate, was also isolated, although not purified to the same extent.

摘要

产气荚膜梭菌的孢子含有至少两种对水解皮层肽聚糖有活性的孢子溶解酶。其中一种酶已被纯化了1800倍,通过在Sephadex G - 75上的色谱法测定其分子量为17400。SDS - PAGE后出现两条明显的蛋白带。对分离出的酶进行了温度、pH、离子强度和酶抑制剂反应以及作用方式的研究。还分离出了第二种酶活性,通过凝胶排阻色谱法测定,其表观分子量(29800)与第一种不同,其最适pH和对皮层底物的活性也不同,不过纯化程度不如第一种。

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