title: Purification of the N-acetylglucosaminide alpha(1-3/4)fucosyltransferase of human milk.
abstract: The N-acetylglucosaminide alpha(1-3/4)fucosyltransferase has been purified 1.8 x 10(6)-fold from human milk by ion-exchange chromatography, affinity chromatography on GDP-agarose and HPLC. The alpha(1-3/4)fucosyltransferase behaves in gel filtration-HPLC as a molecule of M(r) 98,000, and differs from the alpha(1-3)fucosyltransferase which behaves like a molecule of about M(r) 47,000. The enzyme is a glycoprotein, and the purified preparation appears in SDS polyacrylamide gel electrophoresis as a band of M(r) 44,000. The results present the first purification of human milk alpha(1-3/4)fucosyltransferase to apparent homogeneity, and suggest that the alpha(1-3/4)- and alpha(1-3)fucosyltransferase of human milk differ in their native molecular sizes, the former being a dimer of two subunits.
authors.affiliation: Department of Biochemistry, University of Basel, Switzerland.
authors.forename: S
authors.initials: S
authors.lastname: Eppenberger-Castori
authors.forename: H
authors.initials: H
authors.lastname: Lötscher
authors.forename: J
authors.initials: J
authors.lastname: Finne
mesh_terms: D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004187:Disaccharides / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005647:Fucosyltransferases / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D007525:Isoelectric Focusing; D007700:Kinetics; D008895:Milk, Human / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009844:Oligosaccharides / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D004187:Disaccharides; D009844:Oligosaccharides; D005647:Fucosyltransferases; C019818:3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase