Lysosomal Hyaluronidase from Rat Liver

Abstract

The properties of purified liver hyaluronidase have been compared with those of testis hyaluronidase. The lysosomal enzyme showed a similar action pattern to the testis enzyme (1), but had a lower pH optimum at pH 3.5 and reduced affinity for hexasaccharide. The K_m for hyaluronate was 8 x 10^-2 mg per ml. Sodium chloride was not required for enzyme activity but served to prevent inhibition by sulfated polysaccharides, notably chondroitin sulfate B, which had a K_i of 3.8 x 10^-4 mg per ml. The polycation, protamine sulfate, also prevented polyanion inhibition. Liver hyaluronidase, like the testis enzyme (12), exhibited transglycosylase activity.