title: Purification and characterization of alpha (2-6)-sialyltransferase from human liver.
abstract: A Gal beta 1-4GlcNAc alpha (2-6)-sialyltransferase from human liver was purified 34,340-fold with 18% yield by dye chromatography on Cibacron Blue F3GA and cation exchange FPLC. The enzyme preparation was free of other sialyltransferases. It did not contain CMP-NeuAc hydrolase, protease, or sialidase activity, and was stable at -20 degrees C for at least eight months. The donor substrate specificity was examined with CMP-NeuAc analogues modified at C-5 or C-9 of the N-acetylneuraminic acid moiety. Affinity of the human enzyme for parent CMP-NeuAc and each CMP-NeuAc analogue was substantially higher than the corresponding Gal beta 1-4GlcNAc alpha (2-6)-sialyltransferase from rat liver.
authors.affiliation: Institut für Biochemie II, Universität Heidelberg, FRG.
authors.forename: U
authors.initials: U
authors.lastname: Sticher
authors.forename: H J
authors.initials: HJ
authors.lastname: Gross
authors.forename: R
authors.initials: R
authors.lastname: Brossmer
mesh_terms: D002240:Carbohydrate Sequence; D002846:Chromatography, Affinity; D003124:Colorimetry; D003902:Detergents; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D015394:Molecular Structure; D019158:N-Acetylneuraminic Acid; D017830:Octoxynol; D009994:Osmolar Concentration; D011092:Polyethylene Glycols; D012794:Sialic Acids / Q000737:chemistry; D012799:Sialyltransferases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase
chemical_list: D003902:Detergents; D012794:Sialic Acids; D011092:Polyethylene Glycols; D017830:Octoxynol; D012799:Sialyltransferases; D019158:N-Acetylneuraminic Acid; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase