Publications

• Purification to homogeneity of H blood group beta-galactoside alpha 1 leads to 2 fucosyltransferase from porcine submaxillary gland.

  Beyer T.A., Sadler J.E., Hill R.L.

  A beta-galactoside alpha 1 leads to 2 fucosyltransferase has been solubilized from porcine submaxillary glands and purified 124,000-fold to homogeneity by repeated affinity chromatography on GDP-hexanolamine agarose. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of the purified enzyme ... >> More

  A beta-galactoside alpha 1 leads to 2 fucosyltransferase has been solubilized from porcine submaxillary glands and purified 124,000-fold to homogeneity by repeated affinity chromatography on GDP-hexanolamine agarose. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of the purified enzyme revealed two electrophoretic species with apparent Mr = 60,000 and 55,000. The two enzyme species have not been completely resolved, but both appear to be active forms of the fucosyltransferase with approximately equal specific activities. Glycosidase digestion of the fucosylated products with the alpha 1 leads to 2-specific fucosidase from Clostridium perfringens and the alpha 1 leads to 3/alpha 1 leads to 4-specific fucosidase from almond emulsin indicates that the enzyme forms exclusively the Fuc alpha 1 leads to 2Gal linkage with a variety of acceptor substrates. A GDP-fucose hydrolase activity co-purifies with the fucosyltransferase. Identical rates of thermal inactivation and co-migration on gel electrophoresis under nondenaturing conditions suggest that the two activities are due to a single enzyme species. << Less

  J Biol Chem 255:5364-5372(1980) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• Enzymatic properties of the beta-galactoside alpha 1 leads to 2 fucosyltransferase from porcine submaxillary gland.

  Beyer T.A., Hill R.L.

  The acceptor substrate specificity and kinetic properties of the purified porcine submaxillary beta-galactoside alpha 1 leads to 2 fucosyltransferase have been examined. The transferase forms the Fuc alpha 1 leads to 2Gal linkage with oligosaccharides, glycoproteins, and glycolipids which contain ... >> More

  The acceptor substrate specificity and kinetic properties of the purified porcine submaxillary beta-galactoside alpha 1 leads to 2 fucosyltransferase have been examined. The transferase forms the Fuc alpha 1 leads to 2Gal linkage with oligosaccharides, glycoproteins, and glycolipids which contain nonreducing terminal galactose residues and shows no absolute specificity for a particular penultimate residue or for the linkage between the galactose and the penultimate residue. The fucosyltransferase is active in the absence of divalent metal ions, but it is stimulated upon addition of Mn2+, Mg2+, Ca2+, or Co2+. Kinetic analysis indicates an increase in the Km for both donor and acceptor substrates and in the Vmax in the presence of Mn2+. Initial rate studies and inhibition patterns suggest that the transferase has either a rapid equilibrium random kinetic mechanism or a steady state ordered mechanism with GDP-fucose binding first. Human "Bombay" erythrocytes which lack cell surface Fuc alpha 1 leads to 2Gal structures are fucosylated by the transferase, but expression of H blood group activity is dependent on treatment of the cells with neuraminidase. After neuraminidase digestion, the fucosylated cells are serologically identical to native O-type cells. Analysis of the fucosylated material in the erythrocyte membrane on sodium dodecyl sulfate-polyacrylamide gel electrophoresis suggests that fucose is incorporated primarily into glycoprotein acceptors. << Less

  J Biol Chem 255:5373-5379(1980) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• Characterization of three members of murine alpha1,2-fucosyltransferases: change in the expression of the Se gene in the intestine of mice after administration of microbes.

  Lin B., Saito M., Sakakibara Y., Hayashi Y., Yanagisawa M., Iwamori M.

  We cloned three members of a GDP-fucose:beta-galactoside alpha1,2-fucosyltransferase (alpha1,2-fucosyltransferase) family, MFUT-I, -II, and -III, from a cDNA of murine small intestine, and determined their enzymatic properties after transfection of the genes into COS-7 cells, and their expression ... >> More

  We cloned three members of a GDP-fucose:beta-galactoside alpha1,2-fucosyltransferase (alpha1,2-fucosyltransferase) family, MFUT-I, -II, and -III, from a cDNA of murine small intestine, and determined their enzymatic properties after transfection of the genes into COS-7 cells, and their expression in murine tissues by Northern blotting. MFUT-I, -II, and -III exhibited sequence homology with the human H (78.4%), Se (79.0%), and Sec1 (74.9%) gene products, respectively. COS-7 cells transfected with MFUT-I and -II exhibited alpha1,2-fucosyltransferase activity and the best acceptor substrate for both gene products was GA1 to yield a fucosyl GA1 structure, but no activity was detected in COS-7 cells with MFUT-III. MFUT-II yielded a 3.5-kb mRNA transcript in several tissues, whereas MFUT-I and -III were predominantly expressed in epididymis and testis, respectively. The administration of microbes into germ-free mice resulted in a rapid increase of the MFUT-II gene (Se gene) for the synthesis of fucosyl GA1 in the intestine. << Less

  Arch. Biochem. Biophys. 388:207-215(2001) [PubMed] [EuropePMC]

  This publication is cited by 9 other entries.

• Tissue-specific loss of fucosylated glycolipids in mice with targeted deletion of alpha(1,2)fucosyltransferase genes.

  Iwamori M., Domino S.E.

  Glycolipids in epithelial tissues of the gastrointestinal tract act as receptors for enteric bacteria and are implicated in the activation of the intestinal immune system. To clarify the genes involved in the fucosylation of the major glycolipids, substrate glycolipids and fucosylated products wer ... >> More

  Glycolipids in epithelial tissues of the gastrointestinal tract act as receptors for enteric bacteria and are implicated in the activation of the intestinal immune system. To clarify the genes involved in the fucosylation of the major glycolipids, substrate glycolipids and fucosylated products were measured in tissues of wild-type and mutant mice lacking alpha(1,2)fucosyltransferase genes FUT1 or FUT2. Quantitative determination was performed by TLC-immunostaining for GA1 (Gg4Cer), FGA1 (fucosyl GA1), GM1 (II3NeuAc-Gg4Cer), FGM1 (fucosyl GM1), and Forssman glycolipids. Both FGM1 and FGA1 completely disappeared from the antrum, cecum, and colon of FUT2-null mice, but not those of FUT1-null and wild-type mice. Precursor glycolipids, GM1 and GA1, accumulated in tissues of FUT2-null mice, indicating that the FUT2-encoded enzyme preferentially participates in the fucosylation of GA1 and GM1 in these tissues. Female reproductive organs were similarly found to utilize FUT2 for the fucosylation of glycolipids FGA1 (uterus and cervix), and FGM1 (ovary), due to their absence in FUT2-null mice. In FUT1-null mice FGA1 was lost from the pancreas, but was present in wild-type and FUT2-null mice, indicating that FUT1 is essential for fucosylation of GA1 in the pancreas. Ulex europaeus agglutinin-I lectin histochemistry for alpha(1,2)fucose residues confirmed the absence of alpha(1,2)fucose residues from the apical surface of pancreatic acinar glands of FUT1-null mice. Ileum, epididymis, and testis retained specific fucosylated glycolipids, irrespective of targeted deletion of either gene, indicating either compensation for or redundancy of the alpha(1,2)fucosyltransferase genes in these tissues. << Less

  Biochem. J. 380:75-81(2004) [PubMed] [EuropePMC]

  This publication is cited by 5 other entries.