Comparative lectinology: Delineating glycan-specificity profiles of the chicken galectins using neoglycoconjugates in a cell assay
作者： E. M. Rapoport , V. K. Matveeva , H. Kaltner , S. Andre , O. A. Vokhmyanina
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摘要: A major aspect of carbohydrate-dependent galectin functionality is their cross-linking capacity. Using a cell surface as biorelevant platform for binding and panel 40 glycans sensor part fluorescent polyacrylamide neoglycopolymer profiling reactivity, properties related proteins can be comparatively analyzed. The group the chicken galectins (CGs) an especially suited system toward this end due to its relatively small size, compared with mammalian galectins. experiments reveal particularly strong reactivity N-acetyllactosamine repeats all tested CGs shared CG-1A CG-2 histo-blood ABH determinants. In cross-species comparison, CG-1B's closely resembled those human galectin-1, was case galectin-2 (but not galectin-3) ortholog pair. Although binding-site architectures are rather similar, patterns well differ.
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