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Large-scale expression of recombinant sialyttransferases and comparison of their kinetic-properties with native enzymes

Academic Article
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Overview

authors

  • Williams, M. A.
  • Kitagawa, H.
  • Datta, A. K.
  • Paulson, James
  • Jamieson, J. C.

publication date

  • December 1995

journal

  • Glycoconjugate Journal  Journal

abstract

  • Values of Km were determined for three purified sialyltransferases and the corresponding recombinant enzymes. The enzymes were Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase and Gal beta 1-3(4)GlcNAc alpha 2-3 sialyltransferase from rat liver; these enzymes are responsible for the attachment of sialic acid to N-linked oligosaccharide chains; and the Gal beta 1-3GalNAc alpha 2-3 sialyltransferase from porcine submaxillary gland that is responsible for the attachment of sialic acid to O-linked glycoproteins and glycolipids. A procedure for the large scale expression of active sialyltransferases from recombinant baculovirus-infected insect cells is described. For the liver enzymes values of Km were determined using rat and human asialo alpha 1 acid glycoprotein and N-acetyllactosamine as variable substrates; lacto-N-tetraose was also used with the Gal beta 1-3(4)GlcNAc alpha 2-3 sialyltransferases. Antifreeze glycoprotein was used as the macromolecular acceptor for the porcine enzyme. Values for Km were also determined using CMP-NeuAc as the variable substrate.

subject areas

  • Animals
  • Baculoviridae
  • Base Sequence
  • Cloning, Molecular
  • Genetic Vectors
  • Humans
  • Kinetics
  • Liver
  • Molecular Sequence Data
  • Rats
  • Recombinant Proteins
  • Sialyltransferases
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Research

keywords

  • BACULOVIRUS
  • GLYCOPROTEIN
  • SIALYLTRANSFERASE
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Identity

International Standard Serial Number (ISSN)

  • 0282-0080

Digital Object Identifier (DOI)

  • 10.1007/bf00731235

PubMed ID

  • 8748151
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Additional Document Info

start page

  • 755

end page

  • 761

volume

  • 12

issue

  • 6

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