The specificity of proteinases from Streptomyces griseus (pronase)

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 phosphorofluorida...

The proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). Specificity and immobilization of aminopeptidase.

We recently described the purification of two aminopeptidases from Streptomyces griseus (Vosbeck, K.D., Chow, K.-F., and Awad, W.M., Jr. (1973) J. Biol. Chem. 248, 6329-6034). An analysis of the amino acid composition reveals very little differences in the two proteins. Each protein has alanine as the NH2-terminal residue. The aminopeptidases were treated separately with acetic anhydride; as no...

Oxidation of Meloxicam by Streptomyces griseus

The aim of the present investigation was to biotransform the anti-inflammatory compound meloxicam by enzymes present in whole cells of five actinomycete cultures to produce novel bioactive derivatives. Among the actinomycetes screened, Streptomyces griseus NCIM 2622 was found to possess the enzyme system(s) that oxidize meloxicam into two metabolites whereas that present in S. griseus NCIM 2623...

Glutathione S-transferase isoenzymes from Streptomyces griseus.

An inducible, cytosolic glutathione S-transferase (GST) was purified from Streptomyces griseus. GST isoenzymes with pI values of 6.8 and 7.9 used standard GST substrates including 1-chloro-2,4-dinitrobenzene. GST had subunit and native M(r)s of 24 and 48, respectively, and the N-terminal sequence SMILXYWDIIRGLPAH.

Isolation and characterization of a phage active against streptomyces griseus