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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Authors | J P Prieels, D Monnom, J P Perraudin, J Finne, M Burger |
Journal | European journal of biochemistry
(Eur J Biochem)
Vol. 130
Issue 2
Pg. 347-51
(Feb 01 1983)
ISSN: 0014-2956 [Print] England |
PMID | 6687456
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Lectins
- Wheat Germ Agglutinins
- Fucosyltransferases
- Hexosyltransferases
- 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase
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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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