Glycoconjugate Journal

, Volume 9, Issue 6, pp 307–314 | Cite as

Characterization of a glucuronyltransferase: neolactotetraosylceramide glucuronyltransferase from rat brain

  • Chika Kawashima
  • Koji Terayama
  • MasayukiII
  • 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.


glucuronyltransferase HNK-1 antigen rat brain 



glucuronic acid








Nonidet P-40










sulfoglucuronyl glycolipid


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Copyright information

© Chapman & Hall 1992

Authors and Affiliations

  • Chika Kawashima
    • 1
  • Koji Terayama
    • 1
  • MasayukiII
    • 1
  • Shogo Oka
    • 1
  • Toshisuke Kawasaki
    • 1
  1. 1.Department of Biological Chemistry, Faculty of Pharmaceutical SciencesKyoto UniversityKyotoJapan

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