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J. Biol. Chem., Vol. 259, Issue 18, 11208-11214, 09, 1984
C Campbell and P Stanley
Evidence is presented that the GDP-fucose:N-acetyl-glucosaminide 3-
alpha-L-fucosyltransferase activities of two Chinese hamster ovary
glycosylation mutants, LEC11 and LEC12, are structurally distinct enzymes.
The alpha(1,3)fucosyltransferase in LEC12 cell extracts binds to
GDP-hexanolamine-Sepharose and is unaffected by 3 mM N- ethylmaleimide. In
contrast, the alpha(1,3)fucosyltransferase activity in LEC11 cells does not
bind readily to GDP-hexanolamine-Sepharose and is completely inhibited by 1
mM N-ethylmaleimide. The LEC11 and LEC12 alpha(1,3)fucosyltransferases also
differ in the degree to which they are stimulated by divalent cations as
well as in their abilities to fucosylate a variety of exogenous substrates.
Of particular interest is the finding that the LEC11
alpha(1,3)fucosyltransferase adds fucose to certain sialylated
glycoproteins, whereas the LEC12 enzyme is essentially unable to fucosylate
these acceptors, although it is very active with their desialylated
derivatives. The combined evidence shows that the LEC11 and LEC12
alpha(1,3)fucosyltransferase enzymes are different molecules and
presumably, therefore, the products of distinct genes. In addition, neither
of the enzymes appears identical to any of the previously described
alpha(1,3)fucosyltransferase activities from other sources.
The Chinese hamster ovary glycosylation mutants LEC11 and LEC12 express two novel GDP-fucose:N-acetylglucosaminide 3-alpha-L-fucosyltransferase enzymes
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