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Abstract
Connective tissue of the freshwater pulmonate Lymnaea stagnalis was shown to contain fucosyltransferase activity capable of transferring fucose from GDP-Fuc in alpha 1 -2 linkage to terminal Gal of type 3 (Gal beta 1-3GalNAc) acceptors, and in alpha 1-3 linkage to GlcNAc ot type 2 (Gal beta 1-4GlcNAc) acceptors. The alpha 1-2 fucosyltransferase was active with Gal beta 1-3GalNAc beta 1-OCH2CH=CH2 (Km = 12mM, V(max) = 1.3 mUml-1) and Gal beta 1-3GalNAc (km =20 mM, V(max) = 2.1 mUml-1), whereas the alpha 1-3 fucosyltransferase was active with Gal beta 1-4GlcNAc (Km = 23 mM, V(max) = 1.1 mUml-1). The products formed from from Gal beta 1-3GalNAc beta 1-OCH2CH=CH2 and Gal beta 1-4GlcNAc were purified by high performance liquid chromatography, and identified by 500 MHz 1H-NMR spectroscopy and methylation analysis to be Fucalpha1-2Gal beta 1-3GalNAc beta 1-OCH2CH=CH2 and Gal beta 1-4(Fucalpha1-3)GlcNAc, respectively. Competition experiments suggest that the two fucosyltransferase activities are due to two distinct enzymes.
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