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  • Title: The exocellular DD-carboxypeptidase-endopeptidase from Streptomyces albus G. Purification and chemical properties.
    Author: Duez C, Frère JM, Geurts F, Ghuysen JM, Dierickx L, Delcambe L.
    Journal: Biochem J; 1978 Dec 01; 175(3):793-800. PubMed ID: 743235.
    Abstract:
    The exocellular DD-carboxypeptidase-endopeptidase of Streptomyces albus G was purified to protein homogeneity and compared with the exocellular DD-carboxypeptidases-transpeptidases of Streptomyces R61 and Actinomadura R39. The S. albus G enzyme, as it is isolated, occurs in two forms. Enzyme I (30% of the total amount) and enzyme II (70% of the total amount) are identical in all respects, except that, by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate, enzyme I has an apparent mol. wt. (9000) that is half of that found by molecular-sieve filtration under non-denaturing conditions. Irrespective of the technique used, enzyme II has an apparent mol. wt. of about 18500.
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