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Purification of a sialyltransferase from bovine colostrum by affinity chromatography on cdp-agarose

Academic Article
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Overview

authors

  • Paulson, James
  • Beranek, W. E.
  • Hill, R. L.

publication date

  • 1977

journal

  • Journal of Biological Chemistry  Journal

abstract

  • CDP-hexanolamine agarose was used as an affinity adsorbent to purify a CMP-N-acetylneuraminate: beta-D-galactosyl-glycoprotein N-acetylneuraminyltransferase (EC 2.4.99.1) from bovine colostrum. Upon binding of the enzyme to the adsorbent, elution is achieved either nonspecifically, with 0.5 to 1.0 M sodium chloride, or specifically, with CDP. A highly purified sialyltransferase is obtained with a specific activity 440,000 times that of whole colostrum. Fractionation of the purified enzyme by gel filtration gives two species with different molecular weights but equal specific activities toward asialo-alpha1-acid glycoprotein (26.0 to 28.0 micronmol/min/mg of enzyme). The molecular weights of these two forms are about 56,000 and 43,000 as judged by sodium doedcyl sulfate-gel electrophoresis, sedimentation equilibrium, and gel filtration. The catalytic properties of both forms have been examined (Paulson, J. C., Rearick, J. I., and Hill, R. L. (1977) J. Biol. Chem. 252, 2363-2371). It is concluded that the lower molecular weight form may be a partially degraded species of the enzyme of higher molecular weight.

subject areas

  • Animals
  • Cattle
  • Chromatography, Affinity
  • Colostrum
  • Cytosine Nucleotides
  • Drug Stability
  • Female
  • Macromolecular Substances
  • Molecular Weight
  • Pregnancy
  • Sepharose
  • Sialyltransferases
  • Transferases
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 849932
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Additional Document Info

start page

  • 2356

end page

  • 2362

volume

  • 252

issue

  • 7

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