This study establishes the existence of a mammalian buccal mucosal hyaluronidase having properties typical of a lysosomal enzyme. Mucosal hyaluronidase exhibited a distinct substrate preference for hyaluronic acid, generated saturated de-polymerization products by endoglycosidic hydrolysis, and possessed a pH optimum of 3.5 and an isoelectric point of 5.9.
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