Zentralblatt fur Bakteriologie, Mikrobiologie, und Hygiene. Series A, Medical microbiology, infectious diseases, virology, parasitology 1985-Oct
Purification and properties of a proline iminopeptidase from Propionibacterium acnes.
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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 degrees C-55 degrees 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.
