Abstract
1.Clostridium histolyticum collagenase (clostridiopeptidase A, EC 3.4.4.19) was purified by zone electrophoresis on starch and gel-filtration with Sephadex G-200. Two forms of collagenase (I and II) were isolated by subsequent fractionation by DEAE-cellulose column chromatography.2.These two enzymes hydrolyzed collagen at comparable rates, but synthetic peptides and azocoll at different rates.Collagenase II attacked more bonds of collagen than collagenase I.3.Sedimentation constant, molecular weight, electrophoretic mobility, and pH optima for the hydrolysis of collagen and synthetic peptide indicated that collagenases I and II are different enzymes. However, their amino acid compositions were similar.
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