Physicochemical properties and binding-site amino acid residues of galactoside-binding protein of human placenta.
Loading...
Date
1987-03
Journal Title
Journal ISSN
Volume Title
Publisher
Abstract
The galactose-binding lectin of human placenta has been purified to homogeneity
by affinity chromatography on asialo-fetuin column. The protein, extractable from the
tissue only with lactose is apparently membrane-bound. Molecular weight determination of
native protein and subunit indicated a dimer of 13·4 kDa subunits. Inhibition of haemagglutination
with various saccharides indicate that thiodigalactoside is the best inhibitor
followed by lactose· However, p-nitrophenyl- and 1-O-methyl derivatives of galactose
showed that α-anomers inhibited slightly better than β-anomer. Modification of amino acid
residues indicated involvement of arginine, lysine and histidine residues at the saccharidebinding
site. Cysteine residue modificatioin also abolished haemagglutinating activity.
Amino acid composition of the lectin is also presented·
Description
Keywords
Human placenta, galactose-binding lectin, binding-site amino acids, chemical modification
Citation
Nambiar Madhusoodhan P, Basu Debkumar, Appukuttan P S. Physicochemical properties and binding-site amino acid residues of galactoside-binding protein of human placenta. Journal of Biosciences. 1987 Mar; 11(1-4): 331-338.