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LECSTER is the largest, open-access searchable database of lectin characterizations, clinical correlates and citations on the Internet.

Programmed and curated by Peter D'Adamo.

Copyright 2001-2011.

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Total number of records: 619 Matching records: 1

Calystegia sepium : Hedge bindweed

Molecular structure of
Hedge bindweed:Calsepa

Calystegia sepium

Lecster ID:109 Edit Entry
Source Organism:Hedge bindweed
Species:Calystegia sepium
Common Nomenclature:Calsepa
Class:Jacalin-related lectins
Index Nomenclature:LECp.Cal.Sep.rh.Hmm1
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
Source Tissue:Rhizome
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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By Peter D'Adamo. Copyright 2001-2011.