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

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: N-glycosylation of purified rat and rabbit hepatic UDP-glucuronosyltransferases.
    Author: Green MD, Tephly TR.
    Journal: Arch Biochem Biophys; 1989 Aug 15; 273(1):72-8. PubMed ID: 2502948.
    Abstract:
    Five UDP-glucuronosyltransferases (UDPGTs) have been isolated to apparent homogeneity from rat and rabbit liver and have been characterized for their glycoprotein nature by reacting these proteins with commercially available endo- and exoglycosidases. The enzymes studied were rat hepatic p-nitrophenol, 17 beta-hydroxysteroid, and 3 alpha-hydroxysteroid UDPGTs and rabbit hepatic p-nitrophenol and estrone UDPGTs. Hydrolysis of oligosaccharide moieties was evidenced by an increase in the mobility (decreased apparent molecular weight) of the protein subunits after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Purified rabbit hepatic estrone and p-nitrophenol UDPGTs were hydrolyzed by almond glycopeptidase A and endo-beta-N-acetylglucosaminidase H from Streptomyces plicatus (endo H), but not by endo-beta-N-acetylglucosaminidase D from Diplococus pneumoniae (endo D) suggesting that these transferases are glycoproteins of the high mannose type and not of the complex type. Likewise, purified rat hepatic 3 alpha-hydroxysteroid and p-nitrophenol UDPGTs were substrates for glycopeptidase A and endo H but not for endo D. One enzyme, 17 beta-hydroxysteroid UDPGT, was not glycosylated since it was not hydrolyzed by any of the three endoglycosidases. All four glycosylated UDPGTs could serve as substrates for jack bean alpha-mannosidase, confirming the high mannose nature of the oligosaccharide. Deglycosylation of the purified UDPGTs by endo H did not have an effect on the catalytic activities of these proteins.
    [Abstract] [Full Text] [Related] [New Search]