title: Thermodynamic binding studies of galectin-1, -3 and -7.
abstract: The carbohydrate binding specificities of the galectin family of animal lectins has been the source of intense recent investigations. Isothermal titration microcalorimetry (ITC) provides direct determination of the thermodynamics of binding of carbohydrates to lectins, and has provided important insights into the fine carbohydrate binding specificities of a wide number of plant and animal lectins. Recent ITC studies have been performed with galectin-1, galectin-3 and galectin-7 and their interactions with sialylated and non-sialylated carbohydrates. The results show important differences in the specificities of these three galectins toward poly-N-acetyllactosamine epitopes found on the surface of cells.
authors.affiliation: Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY 10461, USA. brewer@aecom.yu.edu
authors.forename: C Fred
authors.initials: CF
authors.lastname: Brewer
mesh_terms: D000818:Animals; D050260:Carbohydrate Metabolism; D002241:Carbohydrates / Q000737:chemistry; D037483:Galectin 1 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D037502:Galectin 3 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D037161:Galectins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D013816:Thermodynamics
chemical_list: D002241:Carbohydrates; D037483:Galectin 1; D037502:Galectin 3; D037161:Galectins; C092525:LGALS7 protein, human