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• W2247246598 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." @default.
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• W2247246598 date "1978-12-01" @default.
• W2247246598 modified "2023-10-03" @default.
• W2247246598 title "The exocellular <scp>dd</scp>-carboxypeptidase-endopeptidase from <i>Streptomyces albus</i> G. Purification and chemical properties" @default.
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• W2247246598 doi "https://doi.org/10.1042/bj1750793" @default.
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