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J. Biol. Chem., Vol. 266, Issue 35, 23648-23653, 12, 1991
J Hirabayashi and K Kasai
The roles of selected amino acid residues of human 14-kDa beta-
galactoside-binding lectin were studied by site-directed mutagenesis. Ten
mutant lectin proteins were produced, in each of which one of the residues
regarded as possibly related to the stability of the lectin (6 cysteine
residues) or one of those highly conserved in the vertebrate
beta-galactoside-binding lectin family (Asn46, Trp68, Glu71, and Arg73),
was substituted. All the mutant lectins in which one of the cysteine
residues had been substituted with serine (C2S, C16S, C42S, C60S, C88S, and
C130S) proved to have sugar binding ability comparable with that of the
wild-type lectin. In addition, one of the mutants in which Cys2 was
substituted (C2S) was found to have become considerably more stable under
non-reducing conditions. It retained asialofetuin binding activity for over
a week in the absence of beta- mercaptoethanol, while the wild-type lectin
lost it within a day. This suggests that oxidation of Cys2 could be a key
process in the inactivation of human 14-kDa lectin. Substitution of highly
conservative Trp68 to tyrosine (W68Y) slightly reduced lactose binding
ability, but the mutant was still adsorbed strongly on asialofetuin-
agarose. Other mutant lectins in which conservative hydrophilic amino acids
were substituted (N46D, E71Q, and R73H) failed to bind to the asialofetuin
agarose, with no sign of retardation. Thus, conservative hydrophilic
residues proved to be more important in carbohydrate recognition than the
cysteine and tryptophan residues, contrary to the widely accepted concept
that these latter residues are essential.
Effect of amino acid substitution by sited-directed mutagenesis on the carbohydrate recognition and stability of human 14-kDa beta-galactoside- binding lectin
Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, Kanagawa, Japan.
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