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DR. D'ADAMO: LECSTER 7


The lectin database of Dr. Peter D'Adamo.
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Calystegia sepium

SPECIES IMAGE
SOURCEHedge bindweed
LECTINSCalsepa
MOLECULAR IMAGE
CLASSJacalin-related lectins
NOMENLECp.Cal.Sep.rh.Hmm1
INDEXPlant lectin / Plant / Rhizome / Hololectins / Mannose/maltose-binding lectins
CHARACTERIZATIONAlthough 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
BIOACTIVITYMitogenicity 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
SOURCE TISSUERhizome
SPECIFICITYMan/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.
INHIBITORSalpha-D-mannopyranoside followed by alpha-D-glucopyranoside. See: Glycoconjug. J. 1997 (14); 259-265
REFERENCESGlycoconj J 1997 Feb;14 (2):259-65
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