Abstract
Previous studies on the in vitro, enzymatic biosynthesis of hyaluronic acid by extracts of calf vitreous hyalocytes have concentrated on the properties of a soluble glycosyl transferase. The present report describes the properties of a particulate glycosyl transferase from hyalocytes and its role in hyaluronic acid biosynthesis. The enzyme catalyzes the incorporation of radioactivity from UDP-[ 14C]glucuronic acid (UDP-[ 14C]GlcUA) and UDP-[ 3H] N-acetylglucosamine (UDP-[ 3H]GlcNAc) into high molecular weight soluble glycosaminoglycan which appears in the reaction medium. In addition, radioactive material is removed from the denatured enzyme by treatment with 1 m-NaCl, 7 m-urea, and leech hyaluronidase. Pronase treatment also solubilizes bound radioactive material. It is proposed that the tightly bound material, solubilized by Pronase or hyaluronidase, may represent the initial formation of enzyme-bound hyaluronic acid, which is subsequently released into the medium following further polymerization.
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