Molecular weight, amino acid composition and physicochemical properties of the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39.
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.
D000596:Amino Acids / Q000032:analysis; D002268:Carboxypeptidases / Q000302:isolation & purification; D002478:Cells, Cultured; D002498:Centrifugation; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D007525:Isoelectric Focusing; D008722:Methods; D008970:Molecular Weight; D002267:Muramoylpentapeptide Carboxypeptidase / Q000032:analysis; D011487:Protein Conformation; D011506:Proteins / Q000032:analysis; D012967:Sodium Dodecyl Sulfate; D013050:Spectrometry, Fluorescence; D013302:Streptomyces / Q000201:enzymology*
D000596:Amino Acids; D011506:Proteins; D012967:Sodium Dodecyl Sulfate; D002268:Carboxypeptidases; D002267:Muramoylpentapeptide Carboxypeptidase