Abstract
The acceptor specificity and general properties of a Lewis blood-group gene associated α-3/4-L-fucosyltransferase isolated from human milk have been examined at the penultimate purification stage involving affinity chromatography on GDP-hexanolamine Sepharose, and after a subsequent gel filtration step on Sephacryl S-200. Both preparations transferred fucose to theO-4 position ofN-acetylglucosamine in Type 1 (Galβ1-3GlcNAc-R) acceptors and theO-3 position of glucose in lactose-based (Galβ1-4Glc) oligosaccharides, and both used Type 1 sialylated compounds when the terminalN-acetylneuraminic acid was present in α-2,3 linkage. The striking difference between the two preparations was in their reactivity with Type 2 (Galβ1-4GlcNAc-R) chains; after Sephacryl S-200 chromatography the apparentK M values for the α-3/4- preparation with unsubstituted low-molecular-weight Type 2 oligosaccharides were considerably increased. Substitution of the terminal galactose with sialic acid in α-2,3 linkage decreased theK M values for low-molecular-weight oligosaccharides but no detectable incorporation of fucose was observed intoN-acetyllactosamine end-groups of glycoproteins withN-linked oligosaccharide chains, irrespective of the presence of sialic acid in the terminal sequences.
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Johnson, P.H., Donald, A.S.R., Feeney, J. et al. Reassessment of the acceptor specificity and general properties of the Lewis blood-group gene associated α-3/4-fucosyltransferase purified from human milk. Glycoconjugate J 9, 251–264 (1992). https://doi.org/10.1007/BF00731137
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DOI: https://doi.org/10.1007/BF00731137