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  • Title: Enzymic properties of an N-acetylglucosaminide 3-alpha-L-fucosyltransferase of a wheat-germ agglutinin-resistant melanoma clone.
    Author: Prieels JP, Monnom D, Perraudin JP, Finne J, Burger M.
    Journal: Eur J Biochem; 1983 Feb 01; 130(2):347-51. PubMed ID: 6687456.
    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.
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