title: [Isolation and properties of 3 Clostridium histolyticum collagenases].
abstract: The collagenases (I, II and III) have been obtained in a highly purified state from fresh cultural medium of Clostridium histolyticum. The collagenases were similar in their properties to clostridiopeptidase A. The three enzymes differed in their molecular weights, isoelectric points and in some chemical properties. Collagenase II exhibited the most potent hydrolytic activity. Its collagenolytic activity was two-fold higher and the peptidase activity was twenty-fold higher as compared with that of collagenase I. All the three enzymes were inactive towards azocasein and were inhibited by EDTA and cysteine.
mesh_terms: D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002850:Chromatography, Gel; D002855:Chromatography, Thin Layer; D003013:Clostridium / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D003012:Microbial Collagenase / Q000302:isolation & purification*; D008970:Molecular Weight
chemical_list: D003012:Microbial Collagenase
vernacular_title: Vydelenie i svoĭstva trekh kollagenaz Clostridium histolyticum.