Summary: Gelatinolytic enzymes secreted by two strains of were partly purified by ammonium sulphate and acetone precipitation and separated by chromatography on G-200 Sephadex. Both were of relatively high molecular weight, were active over a broad pH range and displayed substrate specificity. Both released amino groups from gelatin; one released hydroxyproline too. They may represent a new group of proteolytic enzymes since: (1) though specific for collagenous proteins they attacked only denatured, not native collagen; ana (ii) unlike other recognized proteolytic enzymes they did not attack α-casem.


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