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. 1974 Oct;143(1):233–240. doi: 10.1042/bj1430233

Molecular weight, amino acid composition and physicochemical properties of the exocellular dd-carboxypeptidase–transpeptidase of Streptomyces R39

Jean-Marie Frère 1,3, Ramon Moreno 1,3,*, Jean-Marie Ghuysen 1,3,†, Harold R Perkins 2, Louis Dierickx 1,3, Lucien Delcambe 1,3
PMCID: PMC1168371  PMID: 4464852

Abstract

The exocellular dd-carboxypeptidase–transpeptidase from Streptomyces R39 was purified to protein homogeneity and in milligram amounts. The isolated enzyme consisted of one polypeptide chain of molecular weight about 53300. Its amino acid composition and several physicochemical properties were determined and compared with those of the exo-cellular dd-carboxypeptidase–transpeptidase from Streptomyces R61.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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