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PREPARATION AND SOME CHEMICAL CHARACTERISTICS OF MILK‐CLOTTING PROTEASE FROM BACILLUS MESENTERICUS 76

 

作者: B.K. MESROB,   R.A. VASSILEVA,  

 

期刊: International Journal of Peptide and Protein Research  （WILEY Available online 1981）
卷期: Volume 17, issue 1  

页码: 89-92

 

ISSN:0367-8377

 

年代: 1981

 

DOI:10.1111/j.1399-3011.1981.tb01971.x

 

出版商: Blackwell Publishing Ltd

 

关键词: enzyme;isotachophoresis;metaloenzyme;milk‐clotting;molecular weight;protease

 

数据来源: WILEY

 

摘要:

Pure milk‐clotting protease (MCP‐76) is isolated by isotachophoresis at pH 5.0. The native molecule has only one protein chain. It is a metaloenzyme containing zinc. The pure MCP‐76 has a molecular weight of 33 000 (± 1500) and by diphenyl‐indenonyl‐isothiocyanate method showed arginine as N‐termina

 

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