An assay for α 1,6-Fucosyltransferase (FUT8) activity based on the HPLC separation of a reaction product with fluorescence detection

Hideyuki Ihara, Hiroki Tsukamoto, Naoyuki Taniguchi, Yoshitaka Ikeda

Research output: Chapter in Book/Report/Conference proceedingChapter

4 Citations (Scopus)

Abstract

N-Glycans with an α-fucose unit linked to the 6-position of the innermost GlcNAc are widely distributed among the animal kingdom, from worms and insects to human. This α1,6-linked fucosyl residue, frequently referred to as a core fucose, is formed via the action of an α1,6- fucosyltransferase, the mammalian ortholog which is systematically called FUT8. In mammals, it is well known that the extent of core-fucosylation in cellular and secreted glycoproteins varies, e.g., according to differentiation and carcinogenesis of the cells. This chapter describes a method for the sensitive and quantitative assay of FUT8 activity using a fluorescence-labeled oligosaccharyl asparagine derivative as the glycosyl acceptor substrate.

Original languageEnglish
Title of host publicationGlycosyltransferases
Subtitle of host publicationMethods and Protocols
PublisherHumana Press Inc.
Pages335-348
Number of pages14
ISBN (Print)9781627034647
DOIs
Publication statusPublished - 2013

Publication series

NameMethods in Molecular Biology
Volume1022
ISSN (Print)1064-3745

Keywords

  • 2-Aminopyridine
  • Asn-linked oligosaccharide
  • Core
  • FUT8
  • Fucose
  • Fucosyltransferase
  • Glycoprotein
  • Glycosylation
  • N-glycan
  • Pyridylamine

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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