Abstract
The detailed characterization of a galectin from the toad (Bufo arenarum Hensel) ovary in its primary structure, carbohydrate specificity, and overall biochemical properties has provided novel information pertaining to structural and evolutionary aspects of the galectin family. The lectin consists of identical single-chain polypeptide subunits composed of 134 amino acids (calculated mass, 14,797 daltons), and its N-terminal residue, alanine, is N-acetylated. When compared to the sequences of known galectins, the B. arenarum galectin exhibited the highest identity (48% for the whole molecule and 77% for the carbohydrate recognition domain (CRD)) with the bovine spleen galectin-1, but surprisingly less identity (38% for the whole molecule and 47% for the CRD) with a galectin from Xenopus laevis skin (Marschal, P., Herrmann, J., Leffler, H., Barondes, S. H., and Cooper, D. N. W. (1992) J. Biol. Chem. 267, 12942-12949). Unlike the X. laevis galectin, the binding activity of the B. arenarum galectin for N-acetyllactosamine, the human blood group A tetrasaccharide and Galbeta1,3GalNAc relative to lactose, was in agreement with that observed for the galectin-1 subgroup and those galectins having "conserved" (type I) CRDs (Ahmed, H., a...Continue Reading
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