BIOSYNTHESIS OF THE CHONDROITIN SULFATE-PROTEIN LINKAGE REGION: PURIFICATION AND PROPERTIES OF A GLUCURONOSYLTRANSFERASE FROM EMBRYONIC CHICK BRAIN

Abstract
The present paper describes the purification and properties of a glucuronosyltransferase isolated from 13-day embryonic chick brain. The enzyme catalyzes transfer of glucuronic acid from UDP-glucuronic acid to a series of low and high molecular weight compounds which contain terminal non-reducing beta-D-galactose residues. Studies utilizing enzymatically degraded chondromucoprotein as acceptor suggest that the glucuronosyltransferase terminates biosynthesis of the linkage region between protein and polysaccharide of chondromucoprotein.

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