These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Glucuronosyl transfer to galactose residues in the biosynthesis of HNK-1 antigens and xylose-containing glycosaminoglycans: one or two transferases?
    Author: Curenton T, Ekborg G, Rodén L.
    Journal: Biochem Biophys Res Commun; 1991 Aug 30; 179(1):416-22. PubMed ID: 1715694.
    Abstract:
    An early step in the assembly of the xylose----serine-linked proteoglycans is the transfer of glucuronic acid to the C-3 position of a galactose residue in the carbohydrate-protein linkage region. Since a similar reaction occurs in the biosynthesis of NHK-1 antigens, the question arose whether these processes are catalyzed by the same enzyme. In the present study, the proteoglycan-related glucuronosyltransferase activity in embryonic chick brain was found to be firmly membrane-associated, while the majority of the activity towards N-acetyllactosamine - a model substrate for HNK-1 antigen biosynthesis - was readily solubilized. No activity towards N-acetyllactosamine was found in embryonic chick cartilage, which is a rich source of the proteoglycan-related enzyme. Together with the results of mixed substrate experiments, these findings strongly indicate the existence of two separate glucuronosyltransferases catalyzing transfer to galactose residues.
    [Abstract] [Full Text] [Related] [New Search]