TY - JOUR
T1 - Purification and partial characterization of a mitogenic lectin from vicia sativa
AU - Falasca, A.
AU - Franceschi, C.
AU - Rossi, C. A.
AU - Stirpe, F.
PY - 1979/3/27
Y1 - 1979/3/27
N2 - 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.
AB - 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.
KW - (Vicia sativa, Affinity chromatography)
KW - Hemagglutinin
KW - Lectin
KW - Mitogenicity
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U2 - 10.1016/0005-2795(79)90009-6
DO - 10.1016/0005-2795(79)90009-6
M3 - Article
C2 - 427217
AN - SCOPUS:0018802442
VL - 577
SP - 71
EP - 81
JO - BBA - Protein Structure
JF - BBA - Protein Structure
SN - 0005-2795
IS - 1
ER -