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Characterization of a glucuronyltransferase: neolactotetraosylceramide glucuronyltransferase from rat brain

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Abstract

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.

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Abbreviations

GlcA:

glucuronic acid

Lc-PA14 :

lactotetraose-phenyl-C14H29

nLc-PA14 :

neolactotetraose-phenyl-C14H29

nLcOse4-Cer:

neolactotetraosylceramide

NP-40:

Nonidet P-40

PC:

phosphatidylcholine

PE:

phosphatidylethanolamine

PI:

phosphatidylinositol

PS:

phosphatidylserine

SGGL:

sulfoglucuronyl glycolipid

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Authors and Affiliations

  1. Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, 606-01, Kyoto, Japan

    Chika Kawashima, Koji Terayama,  Masayuki II, Shogo Oka & Toshisuke Kawasaki

Authors
  1. Chika Kawashima
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  2. Koji Terayama
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  3. Masayuki II
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  4. Shogo Oka
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  5. Toshisuke Kawasaki
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Kawashima, C., Terayama, K., Masayuki et al. Characterization of a glucuronyltransferase: neolactotetraosylceramide glucuronyltransferase from rat brain. Glycoconjugate J 9, 307–314 (1992). https://doi.org/10.1007/BF00731091

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  • DOI: https://doi.org/10.1007/BF00731091

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