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.
يمكن للمستخدمين المسجلين فقط ترجمة المقالات
الدخول التسجيل فى الموقع
يتم حفظ الارتباط في الحافظة
الكلمات الدالة
نبذة مختصرة
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.