| Literature DB >> 518555 |
Abstract
The thiol reagent dithiothreitol inhibits the activity of a core GDP-fucose-N-acetylglucosaminide alpha-6-fucosyltransferase in plasma and blood-cell homogenates, while promoting the activity of alpha-2- and alpha-3-fucosyltransferases. The latter enzymes catalyse transfer of fucose on to terminal galactose and subterminal N-acetylglucosamine residues respectively. A thiol-blocking reagent N-ethylmaleimide does not affect the activity of the alpha-6-fucosyltransferase, but inhibits the other two enzymes. These results indicate the presence of a critical disulphide linkage in the alpha-6-fucosyltransferase, and provide a means of delineation of different fucosyltransferases.Entities:
Mesh:
Substances:
Year: 1979 PMID: 518555 PMCID: PMC1161218 DOI: 10.1042/bj1810767
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857