Proteolytic activity of largomycin.
Largomycin, an antibiotic and antitumor protein, purified from the culture broth of Streptomyces pluricolorescens, displayed specific proteolytic activity. Pure largomycin did not degrade a number of substrates commonly used for detection of aminopeptidase, endopeptidase and carboxypeptidase activity. Pure largomycin degraded angiotensin II, bradykinin, a few dipeptides and a number of proteins of KB cell plasma membranes. The biological activity and the proteolytic activity of largomycin showed similar temperature-dependent patterns, suggesting that one protein is responsible for both activities. The apoprotein of largomycin, which did not show antibiotic activity, contained the proteolytic activity.
D000617:Aminoglycosides; D000804:Angiotensin II / Q000378:metabolism; D000900:Anti-Bacterial Agents; D001120:Arginine; D002460:Cell Line; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000378:metabolism*; D013379:Substrate Specificity; D014443:Tyrosine
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D006023:Glycoproteins; D008565:Membrane Proteins; D000804:Angiotensin II; D014443:Tyrosine; C032499:largomycin; D001120:Arginine; D010447:Peptide Hydrolases