Relative affinities of bovine brain 14 kDa galactose lectin binding to individual endogenous gangliosides.
Indian J Biochem Biophys
;
1997 Jun; 34(3): 249-52
Article
in English
| IMSEAR
| ID: sea-29074
ABSTRACT
Sugar-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.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Binding, Competitive
/
Brain
/
Cattle
/
N-Acetylneuraminic Acid
/
Galectins
/
Plant Lectins
/
Electrophoresis, Polyacrylamide Gel
/
Gangliosides
/
Hemagglutinins
/
Lactose
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1997
Type:
Article
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