caa a22 4500 469115033 CHVBK 20180323133122.0 cr unu---uuuuu 170328e19921201xx s 000 0 eng 10.1007/BF00731091 doi (NATIONALLICENCE)springer-10.1007/BF00731091 Characterization of a glucuronyltransferase: neolactotetraosylceramide glucuronyltransferase from rat brain [Elektronische Daten] [Chika Kawashima, Koji Terayama, Masayuki II,, Shogo Oka, Toshisuke Kawasaki] The properties of a rat brain glucuronyltransferase, which is presumed to be associated with the biosynthesis of the HNK-1 epitope on sulfoglucuronyl glycolipids, are described. The enzyme required divalent cations for reaction, with maximal activity at 10mm Mn2+, and exhibited a dual optimum at pH 4-5 and pH 6 depending upon the buffer used, with the highest activity at pH 4.5 in MES buffer. This enzyme strictly recognized the Galβ1-4GlcNAc terminal structure, and was highly specific for neolacto (type 2) glycolipids as acceptor. The enzyme was localized specifically in the brain, and was barely detected in other issues, including the thymus, spleen, liver, kidney, lung, and sciatic nerve fibres. Phosphatidylinositol and phosphatidylserine increased the enzymatic reaction 4.4- and 2.3-fold, respectively, whereas phosphatidylcholine slightly decreased the rate. Chapman & Hall, 1992 glucuronyltransferase nationallicence HNK-1 antigen nationallicence rat brain nationallicence GlcA : glucuronic acid nationallicence Lc-PA14 : lactotetraose-phenyl-C14H29 nationallicence nLc-PA14 : neolactotetraose-phenyl-C14H29 nationallicence nLcOse4-Cer : neolactotetraosylceramide nationallicence NP-40 : Nonidet P-40 nationallicence PC : phosphatidylcholine nationallicence PE : phosphatidylethanolamine nationallicence PI : phosphatidylinositol nationallicence PS : phosphatidylserine nationallicence SGGL : sulfoglucuronyl glycolipid nationallicence Kawashima Chika Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, 606-01, Kyoto, Japan aut Terayama Koji Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, 606-01, Kyoto, Japan aut Masayuki II, Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, 606-01, Kyoto, Japan aut Oka Shogo Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, 606-01, Kyoto, Japan aut Kawasaki Toshisuke Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, 606-01, Kyoto, Japan aut Glycoconjugate Journal Kluwer Academic Publishers 9/6(1992-12-01), 307-314 0282-0080 9:6<307 1992 9 10719 https://doi.org/10.1007/BF00731091 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00731091 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kawashima Chika Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, 606-01, Kyoto, Japan aut NATIONALLICENCE 700 1- Terayama Koji Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, 606-01, Kyoto, Japan aut NATIONALLICENCE 700 1- Masayuki II Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, 606-01, Kyoto, Japan aut NATIONALLICENCE 700 1- Oka Shogo Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, 606-01, Kyoto, Japan aut NATIONALLICENCE 700 1- Kawasaki Toshisuke Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, 606-01, Kyoto, Japan aut NATIONALLICENCE 773 0- Glycoconjugate Journal Kluwer Academic Publishers 9/6(1992-12-01), 307-314 0282-0080 9:6<307 1992 9 10719 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer