Anomer specificity of the 14 kDa galactose-binding lectin: A reappraisal.
Loading...
Date
1995-06
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
Abstract
A β-anomer preference among galactosides has been attributed to the S-type
14 kDa galactose binding lectin. Here the anomeric preference of this lectin from bovine
brain (BBL) is reexamined using inhibition of lectin-mediated haemagglutination, binding
of the lectin to dot-blotted glycoproteins and affinity electrophoresis of the lectin through
polysaccharide-containing gels. 1·0-methyl α-D-galactoside was 8 times better inhibitor of
BBL than the corresponding ß-anomer. The terminal galactose in bovine thyroglobulin
(exclusively. α-linked) were also nearly 8 times more inhibitory than those in asialofetuin
(exclusively ß-linked). The terminal α-galactose-containing endogenous glycoproteins of
bovine brain were nearly 4 times better inhibitors of BBL than laminin. Removal of
terminal α-galactose units by α-galactosidase fully abolished the BBL binding of thyroglobulin
and endogenous glycoproteins. BBL was also sugar-specifically retarded by polyacrylamide
gel containing guar galactommannan which bears only α-linked galactose. Data indicated that
α-galactosides were sometimes better than their β-anomers in binding to BBL. The
significance of this observation to the physiological role of galactose-binding lectins is
discussed.
Description
Keywords
Galactose -binding lectin, α -galactoside, anomer specificity, bovine brain
Citation
Appukuttan P S, Geetha M, Annamma K I. Anomer specificity of the 14 kDa galactose-binding lectin: A reappraisal. Journal of Biosciences. 1995 Jun; 20(3): 377-384.