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|Calystegia sepium : Hedge bindweed|
Molecular structure of
|Lecster ID:109|| Edit Entry |
|Source Organism:||Hedge bindweed|
| Common Nomenclature:||Calsepa|
|Characterization Notes:||Although the lectin strongly reacts with mannose and especially alpha-D-mannopyranoside, the Calystegia lectin is not related to the monocot mannose-binding lectins. See: Glycoconj J 1997 Feb;14 (2):259-65|
|Biological Activity:||Mitogenicity tests have shown that the Calystegia lectin is a powerful T-cell mitogen. Affinity purification of human, plant and fungal glycoproteins on immobilized C. sepium lectin demonstrates that this novel lectin can be used for the isolation of glycoconjugates from various sources. The lectin agglutinates rabbit and human type A erythrocytes. See: Glycoconjug. J. 1997 (14); 259-265|
|Specificity:||Man/maltose (alpha-mannopyranoside>methyl alpha-D-glucpyranoside) The lectin is a dimeric protein composed of two identical non-covalently linked subunits of 16 kDa. Hapten inhibition studies indicate that the novel lectin is best inhibited by maltose and mannose and hence exhibits a sugar binding specificity that differs in some respects from that of all previously isolated plant lectins.|
|Inhibitors:||alpha-D-mannopyranoside followed by alpha-D-glucopyranoside. See: Glycoconjug. J. 1997 (14); 259-265|
|References:||Glycoconj J 1997 Feb;14 (2):259-65|
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