Open AccessBIOSYNTHESIS OF THE CHONDROITIN SULFATE-PROTEIN LINKAGE REGION: PURIFICATION AND PROPERTIES OF A GLUCURONOSYLTRANSFERASE FROM EMBRYONIC CHICK BRAIN
Author(s) -
Alan E. Brandt,
Jack J. Distler,
George W. Jourdian
Publication year - 1969
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.64.1.374
Subject(s) - glucuronic acid , biochemistry , glucuronosyltransferase , biosynthesis , enzyme , chondroitin sulfate , chemistry , glycosyltransferase , biology , polysaccharide , glycosaminoglycan , microsome
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 β-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.