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- W1567285907 abstract "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." @default.
- W1567285907 created "2016-06-24" @default.
- W1567285907 creator A5054008955 @default.
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- W1567285907 date "1986-08-01" @default.
- W1567285907 modified "2023-10-14" @default.
- W1567285907 title "Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian beta-galactosides." @default.
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- W1567285907 doi "https://doi.org/10.1016/s0021-9258(18)67499-x" @default.
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