Characterization of the individual collagenases from Clostridium histolyticum

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Abstract
Six collagenases (.alpha., .beta., .gamma., .delta., .epsilon. and .zeta.), previously isolated from C. histolyticum, were characterized in detail. The MW determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis range from 68,000-125,000. Isoelectric focusing experiments demonstrate that the isoelectric points of the collagenases are in the 5.35-6.20 range. The subspecies of .alpha.- and .gamma.-collagenases (.alpha.1 vs. .alpha.2 and .gamma.1 vs. .gamma.2) have different isoelectric points but the same MW. Microheterogeneity was also observed for the .beta.- and .epsilon.-collagenases. The amino acid compositions of all 6 collagenases were determined, and analysis for neutral sugars and hexosamines shows that none of the enzymes have a significant carbohydrate content. Zn and Ca are the only metals that copurify with the collagenases. The purified enzymes contain .apprx. 1 mol of Zn/mol of protein and a Ca content that varies from .apprx. 2 mol/mol for .alpha.-collagenase to .apprx. 7 mol/mol for .beta.-collagenase. All of the collagenases are 5-10 times more active against gelatin than collagen. The .alpha.-, .beta.- and .gamma.-collagenases are significantly less active toward the synthetic peptide substrates examined than the .delta.-, .epsilon.- and .zeta.-collagenases. C. histolyticum produces 2 distinct classes of collagenase.

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