The binding of fucose-containing glycoproteins by hepatic lectins. Purification of a fucose-binding lectin from rat liver

M. A. Lehrman, R. L. Hill

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41 Scopus citations

Abstract

A lectin with a high affinity for binding ligands through fucose residues has been purified to homogeneity from rat liver. Affinity chromatography of the lectin on fucosyl-bovine serum albumin-agarose is the key step in the purification. Contaminating amounts of a previously described lectin that binds mannose and N-acetylglucosamine are removed from the fucose-binding lectin by either immunoadsorption on anti-mannose/N-acetylglucosamine lectin IgG-agarose or by specific elution of the fucose-binding lectin from fucosyl-bovine serum albumin-agarose. The pure fucose-binding lectin contains two polypeptide subunits with molecular weights of 88,000 and 77,000, respectively, as judged by gel electrophoresis. Peptide maps of the subunits, however, show that they are very similar structurally. In addition, peptide maps show that the fucose lectin is structurally distinct from other rat hepatic lectins. This is supported by the lack of cross-reaction among the different rat liver lectins and their specific antibodies and the inability of specific antibodies to the mannose/N-acetylglucosamine lectin to inhibit the binding of fucosyl-bovine serum albumin by the fucose lectin.

Original languageEnglish (US)
Pages (from-to)7419-7425
Number of pages7
JournalJournal of Biological Chemistry
Volume261
Issue number16
StatePublished - 1986

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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