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SUMMARY Gelatinolytic enzymes secreted by two strains of Mycoplasma arthritidis 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: (i) though specific for collagenous proteins they attacked only denatured, not native, collagen ; and (ii) unlike other recognized proteolytic enzymes they did not attack sc-casein.

Studies on Proteolytic Activity of Mycoplasmas: the Preparation and Properties of Gelatinolytic Enzymes from Strains of Mycoplasma arthritidis