Proteinases of Streptomyces fradiae. I. Preliminary characterization and purification.
A keratinolytic strain of S. fradiae has been shown to synthesize a complex of extracellular proteinases degrading native keratin proteins, elastin and collagen as well as some globular proteins. These enzymes are characterized by basic optimal pH and are inactivated by pheynlmethylsulfonyl fluoride (PMSF). Using preparative polyacrylamide gel electrophoresis, ion-exchange chromatography and affinity chromatography, 6 fractions of active protein of diversified proteolytic activity have been distinguished in the preparation studied.
Galas
E
E
Institute of Technical Biochemistry, Technical University, Stefanowskiego, Poland.
Kaluzewska
T
T
D000595:Amino Acid Sequence; D000818:Animals; D002852:Chromatography, Ion Exchange; D003094:Collagen / Q000378:metabolism; D004549:Elastin / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007633:Keratins / Q000378:metabolism; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity
D010455:Peptides; D007633:Keratins; D003094:Collagen; D004549:Elastin; D010450:Endopeptidases