The Mode of Action of an Alkaline Proteinase from Streptomyces griseus on Baker's Yeast Cytochrome c

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In order to elucidate the specificity of the alkaline proteinase from Streptomyces griseus (ATCC 3463) on protein substrates of known primary structures, baker's yeast (Saccharomyces oaiformis) cytochrome c was used. The peptides in the hydrolyzate of the NES-cytochrome c were fractionated by chromatography on a column of Dowex 50×2 into thirtyeight peaks. Most of the peaks were not homogeneous and they were separated totally into sixty-six peptides and six free amino acids.
The amino acid and the N-terminal analyses of these peptides were carried out to find the exact positions to locate these peptides in the linear structure of the cytochrome. All the isolated peptides could be located in the known primary structure of the cytochrome without inconsistency. The alkaline proteinase hydrolyzed quickly the arginyl, lysyl, histidyl, phenylalanyl, tyrosyl, asparaginyl, leucyl, methionyl, and alanyl linkages, but not prolyl, aspartyl and cystinyl bonds in the cytochrome c. Therefore the enzyme possesses quite a broad specificity.