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Anomer specificity of the 14 kDa galactose-binding lectin: A reappraisal

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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.

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Abbreviations

L-14:

14 kDa galactose-binding lectin

BBL:

bovine brain 14 kDa galactose binding lectin: PBS. 20mM potassium phosphate buffer, pH 7.4 containing 150mM NaCl

HRP:

horse radish peroxidase

TAG:

terminal α-linked galactose

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Authors and Affiliations

  1. Neurochemistry division sree chitra Tirunal Institute for Medical Science and Technology, 695 001, Trivandrum, India

    P. S. Appukuttan, M. Geetha & K. I. Annamma

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  1. P. S. Appukuttan
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  2. M. Geetha
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  3. K. I. Annamma
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Appukuttan, P.S., Geetha, M. & Annamma, K.I. Anomer specificity of the 14 kDa galactose-binding lectin: A reappraisal. J Biosci 20, 377–384 (1995). https://doi.org/10.1007/BF02703841

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  • DOI: https://doi.org/10.1007/BF02703841

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