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Transfer of synthetic sialic-acid analogs to n-linked and o-linked glycoprotein glycans using 4 different mammalian sialytransferases

Academic Article
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Overview

authors

  • Gross, H. J.
  • Rose, U.
  • Krause, J. M.
  • Paulson, James
  • Schmid, K.
  • Feeney, R. E.
  • Brossmer, R.

publication date

  • September 1989

journal

  • Biochemistry  Journal

abstract

  • This paper presents kinetic properties of the transfer of several synthetic 9-substituted sialic acid analogues onto N- or O-linked glycoprotein glycans by four purified mammalian sialyltransferases: Gal beta 1,4GlcNac alpha 2,6sialyltransferase, Gal beta-1,4(3)GlcNAc alpha 2,3-sialyltransferase, Gal beta 1,3GalNAc alpha 2,3sialyltransferase, and GalNAc alpha 2,6sialyltransferase. The substituents at C-9 of the sialic acid analogues introduce special biochemical characteristics: 9-Amino-NeuAc represents, up to the present, the first derivative that is resistant toward bacterial, viral, and mammalian sialidases but is transferred by a sialyltransferase. 9-Acetamido-NeuAc, 9-benzamido-NeuAc, and 9-hexanoylamido-NeuAc differ in size and hydrophobic character from each other and from parent NeuAc. 9-Azido-NeuAc may be used to introduce a photoreactive label. The kinetic properties of the four sialyltransferases with regard to the donor CMP-glycosides differed distinctly depending on the structure of the substituent at C-9. CMP-9-amino-NeuAc was only accepted as donor substrate by Gal beta 1,4GlcNAc alpha 2,6sialyltransferase (rat liver), but the Km value was 14-fold higher than that of parent CMP-NeuAc. In contrast, 9-azido-NeuAc was readily transferred by each of these four enzymes. 9-Acetamido-NeuAc, which is a receptor analogue for influenza C virus, 9-benzamido-NeuAc, and 9-hexanoylamido-NeuAc were also accepted by each sialyltransferase, but incorporation values differed significantly depending on the enzyme used. For the first time, the resialylation of asialo-alpha 1-acid glycoprotein with 9-substituted sialic acid analogues by Gal beta 1,4GlcNAc alpha 2,6sialyltransferase is demonstrated.

subject areas

  • Animals
  • Chromatography, High Pressure Liquid
  • Galactosidases
  • Glycoproteins
  • Hydrogen-Ion Concentration
  • Isoelectric Focusing
  • Kinetics
  • Liver
  • Polysaccharides
  • Rats
  • Sialic Acids
  • Sialyltransferases
  • Swine
  • beta-Galactosidase
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Identity

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi00444a036

PubMed ID

  • 2510824
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Additional Document Info

start page

  • 7386

end page

  • 7392

volume

  • 28

issue

  • 18

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