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 language | English (US) |
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Pages (from-to) | 967-976 |
Number of pages | 10 |
Journal | Glycoconjugate Journal |
Volume | 13 |
Issue number | 6 |
DOIs | |
State | Published - 1996 |
Externally published | Yes |
Keywords
- Actin
- Actin-binding proteins
- Calreticulin
- Lectin
- Ovine
- Placental
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology