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Enzymic properties of an N-acetylglucosaminide 3-alpha-L-fucosyltransferase of a wheat-germ agglutinin-resistant melanoma clone.

Abstract
A fucosyltransferase was solubilized by extraction with Triton CF-54 from a wheat-germ agglutinin-resistant variant of mouse B16 melanoma. Through affinity chromatography on GDP hexanolamine--Sepharose a 44-fold enrichment of its specific activity was obtained. Analysis of its specificity indicated that the enzyme is an N-acetylglucosaminide 3-alpha-L-fucosyltransferase, which is able to transfer fucose to oligosaccharides containing Gal(beta 1-4)GlcNAc and Gal(beta 1-4)Glc structures. The enzyme is activated by divalent cations and has a maximum of activity at pH 5. It is unable to transfer fucose to sialylated glycoproteins, 6-alpha-sialyllactose or 3-alpha-sialyllactose. As suggested by its precipitation in the presence of antibodies raised in rabbit against a soluble human milk N-acetylglucosaminide 3-alpha-L-fucosyltransferase, these two enzymes seem to be structurally related.
AuthorsJ P Prieels, D Monnom, J P Perraudin, J Finne, M Burger
JournalEuropean journal of biochemistry (Eur J Biochem) Vol. 130 Issue 2 Pg. 347-51 (Feb 01 1983) ISSN: 0014-2956 [Print] England
PMID6687456 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Lectins
  • Wheat Germ Agglutinins
  • Fucosyltransferases
  • Hexosyltransferases
  • 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase
Topics
  • Agglutination Tests
  • Animals
  • Chemical Phenomena
  • Chemistry
  • Clone Cells
  • Drug Resistance
  • Enzyme Activation (drug effects)
  • Fucosyltransferases (isolation & purification)
  • Hexosyltransferases (isolation & purification)
  • Lectins (pharmacology)
  • Melanoma (enzymology)
  • Mice
  • Neoplasms, Experimental (enzymology)
  • Solubility
  • Wheat Germ Agglutinins

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