“…Whereas stronger lactose binding has been reported for some galectins, such as galectin-8, [22] stronger binding of galectin-1, galectin-2, and galectin-3 to lactose than to LacNAc contrasts with previous findings and is presumably assay-specific, as is commonly observed for glycan analysis and microarray experiments. [21,25,41] The binding preferences of galectins established here emphasize that distinct glycosylations on the basic lactose or LacNAc motifs are extremely important for targeted galectin binding, because sugar residues adjacent to basic motifs alter galectin affinity most drastically (Figure 4). In particular, 3'-Oglycosylations of LacNAc, including 3'-O-b galactosidation of lactose as well as (aÀ)blood group glycosylations and a-mannosylation, strongly enhanced binding of most galectins.…”