CHARACTERIZATION AND ACTIVE FRAGMENT OF PHENOMYCIN, AN ANTITUMOR POLYPEPTIDE ANTIBIOTIC

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Abstract

The amino acid composition and molecular weight of phenomycin and degradation studies are reported in this paper. By STEIN-MOORE'S and ultraviolet absorption methods, the molar ratio of amino acids in phenomycin were determined. The N-terminal amino acid is aspartic acid or asparagine.The C-terminal amino acid, determined with carboxypeptidase A and by hydrazinolysis, is tryptophan. The molecular weight is estimated to be about 10, 000 by ARCHIBALD'S method and from the amino acid analysis. The presence of D-amino acids in phenomycin is not certain. Proteolytic enzymes, pepsin, trypsin, chymotrypsin, pronase, nagarse and papain, digest and inactivate phenomycin. One of the fragments obtained by cyanogen bromide cleavage inhibits protein synthesis in a cell-free system of EHRLICH carcinoma cells almost as effectively as phenomycin.

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