Studies on sulphatases. 18. Preparation of chondroitinase-free chondrosulphatase from extracts of Proteus vulgaris

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Abstract
The chondrosulfatase of P. vulgaris N.C.T.C. no. 4636 was separated from the associated chondroitinase by selective adsorption on calcium phosphate gel under strictly controlled experimental conditions. The chondrosulfatase subsequently eluted from the gel shows negligible activity towards the polymerized form of chondroitin sulfate, but is very active towards chondroitin sulfate which has been exhaustively degraded by testicular hyaluronidase. Chondroitinase activity is in no way dependent on a preliminary hydrolysis of ester sulfate groups by chondrosulfatase, since when preparations containing both enzymes are incubated with polymerized chondroitin sulfate in the presence of phosphate ions, the sulfatase activity is completely inhibited whereas chondroitinase activity is not affected.