Abstract
Proline iminopeptidase was extracted from the cells of a strain of Propionibacterium acnes and purified. The molecular weight was estimated to be about 120,000 by SDS-polyacrylamide gel electrophoresis. The enzyme showed the highest activity at 50°C–55°C and its optimum pH was found at 7.5–8.0. The enzyme activity was inhibited by p-chloromercuribenzoate, indicating that this peptidase is a SH-enzyme. Especially prolyl-glycyl-glycine but also prolyl-proline bonds were hydrolyzed by this enzyme, glycyl-proline was not split.
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Schedule a callMore From: Zentralblatt für Bakteriologie, Mikrobiologie und Hygiene / A: Medical Microbiology, Infectious Diseases, Virology, Parasitology
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