A sialic acid-binding lectin from ovine placenta: Purification, specificity and interaction with actin

M. Mercedes Iglesias, Gisela D. Cymes, Carlota Wolfenstein-Todel

Research output: Contribution to journalArticlepeer-review

Abstract

A sialic-acid-specific lectin from ovine placental cotyledons was purified by affinity chromatography on bovine submaxillary mucin-agarose followed by gel filtration, and it showed a molecular weight of 65,000 by sodium dodecylsulfate-polyacrylamide gel electrophoresis. This lectin has the capacity to interact with actin, since it binds to actin-F in a cosedimentation assay and it acts as a mediator in the binding of actin to the affinity column. The lectin agglutinated rabbit and rat erythrocytes, but not human A, B or O erythrocytes. Haemagglutination inhibition assays of different saccharides, glycoproteins and glycolipids indicate that this lectin has affinity for sialic acid, which is enhanced by its O-acetylation. The N-terminal sequence of the protein shows 92% identity with rabbit and porcine uterine calreticulin.

Original languageEnglish (US)
Pages (from-to)967-976
Number of pages10
JournalGlycoconjugate Journal
Volume13
Issue number6
DOIs
StatePublished - Jan 1 1996
Externally publishedYes

Keywords

  • Actin
  • Actin-binding proteins
  • Calreticulin
  • Lectin
  • Ovine
  • Placental

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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