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须癣毛癣菌刺猬变种胞外蛋白酶的部分纯化及动力学研究

Partial purification and kinetic studies of exocellular proteinase from Trichophyton mentagrophytes var. erinacei.

作者信息

Aubaid A H, Muhsin T M

机构信息

Medicine Department, Technical Institute, Nassyria, Iraq.

出版信息

Mycoses. 1998 Mar-Apr;41(3-4):163-8. doi: 10.1111/j.1439-0507.1998.tb00318.x.

DOI:10.1111/j.1439-0507.1998.tb00318.x
PMID:9670769
Abstract

The dermatophyte Trichophyton mentagrophytes var. erinacei isolated from a patient with tinea cruris was cultured in peptone-glucose broth from which an exocellular proteinase was obtained. The enzyme was partly purified by Sephadex G-100 gel filtration. Its molecular weight was determined to be 33,000 on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimal pH was 8.5, the optimal temperature 35 degrees C. The proteolytic activity was specifically increased against casein and inhibited by phenylmethylsulphonyl fluoride. The enzyme was identified as alkaline serine proteinase.

摘要

从一名股癣患者身上分离出的须癣毛癣菌变种——猬毛癣菌,在蛋白胨-葡萄糖肉汤中培养,从中获得了一种胞外蛋白酶。该酶通过Sephadex G-100凝胶过滤进行了部分纯化。在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)上测定其分子量为33000。最适pH为8.5,最适温度为35℃。其蛋白水解活性针对酪蛋白有特异性增强,且被苯甲基磺酰氟抑制。该酶被鉴定为碱性丝氨酸蛋白酶。

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