Antigenicity 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...

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

Genetic recombination in Streptomyces griseus.

Low-frequency (10(-6)) genetic recombination was observed in a cephamycin-producing strain of Streptomyces griseus. The recombinants were predominantly heteroclones. Heteroclone analysis was performed involving four heteroclones of one cross. In 100 mutants correlation was found between the type of auxotrophy and the level of antibiotic activity. A cross of this strain with a streptomycin-produ...