Biosynthesis of the chondroitin sulfate-protein linkage region: purification and properties of a glucuronosyltransferase from embryonic chick brain.
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.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002247:Carbon Isotopes; D002642:Chick Embryo; D002807:Chondroitin / Q000096:biosynthesis*; D002848:Chromatography, DEAE-Cellulose; D005965:Glucuronates / Q000378:metabolism*; D005966:Glucuronidase / Q000378:metabolism; D011485:Protein Binding; D014166:Transferases / Q000302:isolation & purification*
D002247:Carbon Isotopes; D005965:Glucuronates; D002807:Chondroitin; D014166:Transferases; D005966:Glucuronidase