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Isolation and properties of 3 Clostridium histolyticum collagenases

Solov'eva, N.I.; Balaevskaia, T.O.; Makeeva, O.S.; Orekhovich, V.N.

Voprosy Meditsinskoi Khimii 26(5): 674-677

1980

ISSN/ISBN: 0042-8809
PMID: 6252691
Document Number: 162897
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.

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