The exocellular DD-carboxypeptidase-endopeptidase from Streptomyces albus G. Purification and chemical properties.
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.
D000409:Alanine; D000596:Amino Acids / Q000032:analysis; D002850:Chromatography, Gel; D004150:Dipeptidases; D004151:Dipeptides; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification; D005110:Extracellular Space / Q000201:enzymology; D008970:Molecular Weight; D013057:Spectrum Analysis; D013302:Streptomyces / Q000201:enzymology*
D000596:Amino Acids; D004151:Dipeptides; D010450:Endopeptidases; D004150:Dipeptidases; C019989:DD-carboxypeptidase-endopeptidase; D000409:Alanine