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J. Biol. Chem., Vol. 261, Issue 22, 10119-10126, 08, 1986
H Leffler and SH Barondes
Binding of a series of mammalian glycoconjugates to three soluble rat lung
lectins was determined with a quantitative assay. The three lectins,
RL-14.5, RL-18, and RL-29, had a similar apparent affinity for lactose and
associated with the same critical determinants, which included positions 4
and 6 of Gal and part of Glc. Derivatization at position 3 of Glc in
lactose markedly reduced reactivity with the three lectins. For RL-14.5 and
RL-29 the determinant extended specifically to the 3-hydroxyl of Glc which
must be equatorial. In contrast, the stereochemical requirements for RL-18
were less specific, and Gal beta 1-3GalNAc bound as well as lactose. For
RL-29 activity was markedly enhanced by GalNAc alpha 1-3 substitution on
Gal, a modification which had little effect with RL-18 and inhibited
binding to RL-14.5. Combinations of these residues in larger
oligosaccharides and glycopeptides did not substantially enhance binding
above that which might be expected from the sum of the constituent
beta-galactoside residues. Although these lectins showed overlapping
specificities, their binding properties are sufficiently different to
suggest selective interactions with naturally occurring mammalian
glycoconjugates.
Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian beta-galactosides
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