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Purification to homogeneity of a beta-galactoside alpha-2- 3 sialytransferase and partial-purification of an alpha-n-acetylgalactosaminide alpha-2- 6 sialytransferase from porcine sub-maxillary glands

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Overview

authors

  • Sadler, J. E.
  • Rearick, J. I.
  • Paulson, James
  • Hill, R. L.

publication date

  • 1979

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Two different sialyltransferases (EC 2.4.99.1) have been resolved from Triton X-100 extracts of porcine submaxillary glands by affinity chromatography on CDP-hexanolamine agarose. The predominant sialyltransferase of this tissue, a CMP-N-acetylneuraminate: alpha-D-N-acetylgalactosaminide alpha2 leads to 6 sialyltransferase, has been obtained in a partially purified and stable form. A less abundant but highly active enzyme, a CMP-N-acetylneuraminate: beta-D-galactoside alpha2 leads to 3 sialyltransferase, was purified over 90,000-fold to homogeneity. Chromatography of the latter enzyme on Sephadex G-200 separated two noninterconverting forms, designated A and B, with Stokes radii of 51 A and 31 A, respectively. Both forms have equal specific activity toward lactose and contain a single polypeptide with a molecular weight of about 50,000 as estimated by gel electrophoresis. Form A appears to bind 1.18 g of Triton X-100 per g of protein, or nearly an entire detergent micelle per polypeptide, while Form B binds little or no detergent. The enzymatic properties of both forms are similar (Rearick, J.I., Sadler, J.E., Paulson, J.C., and Hill, R.L. (1979) J. Biol. Chem. 254, 4444-4451) supporting the conclusion that Form A may represent the native sialyltransferase with an intact membrane-binding site, and Form B may be a large proteolytic fragment of Form A.

subject areas

  • Acetylgalactosamine
  • Animals
  • Galactosides
  • Kinetics
  • Molecular Conformation
  • Sialyltransferases
  • Submandibular Gland
  • Substrate Specificity
  • Swine
  • Transferases
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 438196
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Additional Document Info

start page

  • 4434

end page

  • 4442

volume

  • 254

issue

  • 11

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