caa a22 4500 469115343 CHVBK 20180323133123.0 cr unu---uuuuu 170328e19921001xx s 000 0 eng 10.1007/BF00731137 doi (NATIONALLICENCE)springer-10.1007/BF00731137 Reassessment of the acceptor specificity and general properties of the Lewis blood-group gene associated α-3/4-fucosyltransferase purified from human milk [Elektronische Daten] [Philip Johnson, Alastair Donald, James Feeney, Winifred Watkins] 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. Chapman & Hall, 1992 α-3/4- L -fucosyltransferase nationallicence Lewis blood-group gene encoded enzyme nationallicence Lewis antigens nationallicence sialyl-Lea nationallicence X-antigen nationallicence sialyl-X antigen nationallicence human milk nationallicence Johnson Philip Division of Immunochemical Genetics, MRC Clinical Research Centre, Watford Road, HA1 3UJ, Harrow, Middlesex, UK aut Donald Alastair Division of Immunochemical Genetics, MRC Clinical Research Centre, Watford Road, HA1 3UJ, Harrow, Middlesex, UK aut Feeney James Biomedical Nuclear Magnetic Resonance Centre, National Institute for Medical Research, Mill Hill, NW7 1AA, London, UK aut Watkins Winifred Division of Immunochemical Genetics, MRC Clinical Research Centre, Watford Road, HA1 3UJ, Harrow, Middlesex, UK aut Glycoconjugate Journal Kluwer Academic Publishers 9/5(1992-10-01), 251-264 0282-0080 9:5<251 1992 9 10719 https://doi.org/10.1007/BF00731137 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00731137 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Johnson Philip Division of Immunochemical Genetics, MRC Clinical Research Centre, Watford Road, HA1 3UJ, Harrow, Middlesex, UK aut NATIONALLICENCE 700 1- Donald Alastair Division of Immunochemical Genetics, MRC Clinical Research Centre, Watford Road, HA1 3UJ, Harrow, Middlesex, UK aut NATIONALLICENCE 700 1- Feeney James Biomedical Nuclear Magnetic Resonance Centre, National Institute for Medical Research, Mill Hill, NW7 1AA, London, UK aut NATIONALLICENCE 700 1- Watkins Winifred Division of Immunochemical Genetics, MRC Clinical Research Centre, Watford Road, HA1 3UJ, Harrow, Middlesex, UK aut NATIONALLICENCE 773 0- Glycoconjugate Journal Kluwer Academic Publishers 9/5(1992-10-01), 251-264 0282-0080 9:5<251 1992 9 10719 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer