Abstract
From the seeds of Vicia sativa a lectin has been purified by affinity chromatography on Sephadex G-100, followed by specific elution with D-glucose. The lectin is a glycoprotein with a molecular weight of 70 000. The aminoacid composition and the total sugar content have been determined. This lectin agglutinates horse, rabbit and human erythrocytes, with no specificity for human blood groups, but does not agglutinate calf and sheep erythrocytes. The agglutinating activity is inhibited by mono-, di-, and trisaccharides with a pyranosyl residue whose free hydroxyl group in position 4 has the configuration of glucose, and by fructose. The lectin has mitogenic activity on human peripheral blood lymphocytes.
| Original language | English |
|---|---|
| Pages (from-to) | 71-81 |
| Number of pages | 11 |
| Journal | BBA - Protein Structure |
| Volume | 577 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Mar 27 1979 |
Keywords
- (Vicia sativa, Affinity chromatography)
- Hemagglutinin
- Lectin
- Mitogenicity
ASJC Scopus subject areas
- Medicine(all)
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Falasca, A., Franceschi, C., Rossi, C. A., & Stirpe, F. (1979). Purification and partial characterization of a mitogenic lectin from vicia sativa. BBA - Protein Structure, 577(1), 71-81. https://doi.org/10.1016/0005-2795(79)90009-6