The specificity of proteinases from Streptomyces griseus (pronase).
Purification of pronase by ion-exchange chromatography gave four proteolytically active fractions. Fraction A(2) contained an endopeptidase that attacks poly l-valine. Fraction B contained an endopeptidase, an aminopeptidase and carboxypeptidases. The activities against hippuryl-l-arginine and hippuryl-l-phenylalanine could be inhibited to a considerable extent by di-isopropyl phosphorofluoridate and by EDTA. Fraction C contained an endopeptidase resembling bovine trypsin. The pure enzyme was completely inactivated by di-isopropyl phosphorofluoridate and pancreatic trypsin inhibitor and to about 90% by other naturally occurring trypsin inhibitors. Fraction D contained an apparently homogeneous endopeptidase, inhibited by diisopropyl phosphorofluoridate, that adsorbed to and hydrolysed elastin. The activity of all these fractions was tested qualitatively against a wide range of small peptides and synthetic substrates.
D000626:Aminopeptidases / Q000032:analysis; D001120:Arginine / Q000378:metabolism; D002268:Carboxypeptidases / Q000032:analysis; D002852:Chromatography, Ion Exchange; D004492:Edetic Acid / Q000494:pharmacology; D004549:Elastin / Q000378:metabolism; D006626:Hippurates / Q000378:metabolism; D007531:Isoflurophate / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000032:analysis*; D010649:Phenylalanine / Q000378:metabolism; D011480:Protease Inhibitors; D013302:Streptomyces / Q000201:enzymology*; D014357:Trypsin / Q000032:analysis; D014361:Trypsin Inhibitors / Q000494:pharmacology; D014633:Valine / Q000378:metabolism
D006626:Hippurates; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D007531:Isoflurophate; D010649:Phenylalanine; D004549:Elastin; D001120:Arginine; D004492:Edetic Acid; D002268:Carboxypeptidases; D010447:Peptide Hydrolases; D000626:Aminopeptidases; D014357:Trypsin; D014633:Valine