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链霉菌R61胞外DD-羧肽酶-转肽酶的分子量及氨基酸组成

Molecular weight and amino acid composition of the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61.

作者信息

Frère J M, Ghuysen J M, Perkins H R, Nieto M

出版信息

Biochem J. 1973 Nov;135(3):463-8. doi: 10.1042/bj1350463.

Abstract

A procedure allowing the purification of milligram amounts of the exocellular dd-carboxypeptidase-transpeptidase from Streptomyces R61 to protein homogeneity (95% purity) is described. The isolated protein has a molecular weight of about 38000 and consists of one polypeptide chain. Its amino acid composition is presented.

摘要

本文描述了一种从链霉菌R61中纯化毫克量胞外dd-羧肽酶-转肽酶至蛋白质均一性(纯度95%)的方法。分离得到的蛋白质分子量约为38000,由一条多肽链组成。文中给出了其氨基酸组成。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ee15/1165848/10ada6c48197/biochemj00597-0098-a.jpg

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本文引用的文献

1
The oxidation of ribonuclease with performic acid.
J Biol Chem. 1956 Apr;219(2):611-21.
3
Penicillin-sensitive DD-carboxypeptidases from Streptomyces strains R39 and K11.
Biochemistry. 1972 Mar 28;11(7):1290-8. doi: 10.1021/bi00757a027.
4
Penicillin-sensitive DD-carboxypeptidase from Streptomyces strain R 61.
Biochemistry. 1971 May 25;10(11):2163-70. doi: 10.1021/bi00787a032.
9
Peptide inhibitors of Streptomyces DD-carboxypeptidases.
Biochem J. 1973 Jan;131(1):163-71. doi: 10.1042/bj1310163.
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Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.
Proc Natl Acad Sci U S A. 1972 Mar;69(3):662-6. doi: 10.1073/pnas.69.3.662.

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