Relative affinities of bovine brain 14 kDa galactose lectin binding to individual endogenous gangliosides

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dc.contributorKannan, VM
dc.contributorAppukuttan, PS
dc.date.accessioned2012-12-04T11:45:05Z
dc.date.available2012-12-04T11:45:05Z
dc.date.issued1997
dc.description.abstractSugar-specific binding of bovine brain 14 kDa galactose-binding lectin (BBL) to individual endogenous gangliosides (GM1, GM2, GD1a, GD1b and GT1b) was studied using affinity electrophoresis of ganglioside-lectin mixture in polyacrylamide gel at pH 8.3. Unbound (free) lectin moved ahead while ganglioside-lectin complex moved very little. Sugar-specificity of binding was confirmed by reversal of the interaction by (i) presence of lactose along with the lectin and (ii) pretreatment of gangliosides with another galactose-binding lectin, Ricinus communis agglutinin. Stoichiometry of ganglioside-BBL interaction revealed that GT1b had the highest affinity for the lectin followed by GD1b and GM2, while GM1 and GD1a had the least affinity. Results indicated that a terminal sialic acid moiety covering a galactose moiety may at times enhance BBL recognition of the latter and that changes in ganglioside pattern is a possible modulator of lectin function in vivo.
dc.identifier.citationINDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS. 34; 3; 249-252en_US
dc.identifier.urihttps://dspace.sctimst.ac.in/handle/123456789/979
dc.publisherINDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS
dc.subjectBiochemistry
dc.titleRelative affinities of bovine brain 14 kDa galactose lectin binding to individual endogenous gangliosides
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