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Energetics of carbohydrate binding by a 14 kDa S-type mammalian lectin

Ramkumar, R and Surolia, A and Podder, SK (1995) Energetics of carbohydrate binding by a 14 kDa S-type mammalian lectin. In: Biochemical Journal, 308 (Pt 1). pp. 237-241.

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Official URL: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC113686...


The thermodynamics of the binding of derivatives of galactose and lactose to a 14 kDa beta-galactoside-binding lectin (L-14) from sheep spleen has been studied in 10 nM phosphate/150 mM NaCl/10 mM beta-mercaptoethanol buffer, pH 7.4, and in the temperature range 285-300 K using titration calorimetry. The single-site binding constants of various sugars for the lectin were in the following order: N-acetyl-lactosamine thiodigalactoside > 4-methylumbelliferyl lactoside > lactose > 4-methylumbelliferyl alpha-D-galactoside > methyl-alpha-galactose > methyl-beta-galactose. Reactions were essentially enthalpically driven with the binding enthalpies ranging from -53.8 kJ/mol for thiodigalactoside at 301 K to -2.2 kJ/mol for galactose at 300 K, indicating that hydrogen-bonding and van der Waals interactions provide the major stabilization for these reactions. However, the binding of 4-methylumbelliferyl-alpha-D-galactose displays relatively favourable entropic contributions, indicating the existence of a non-polar site adjacent to the galactose-binding subsite. From the increments in the enthalpies for the binding of lactose, N-acetyl-lactosamine and thiodigalactoside relative to methyl-beta-galactose, the contribution of glucose binding in the subsite adjacent to that for galactose shows that glucose makes a major contribution to the stability of L-14 disaccharide complexes. Observation of enthalpy-entropy compensation for the recognition of saccharides such as lactose by L-14 and the absence of it for monosaccharides such as galactose, together with the lack of appreciable changes in the heat capacity (delta Cp), indicate that reorganization of water plays an important role in these reactions.

Item Type: Journal Article
Publication: Biochemical Journal
Publisher: Portland Press
Additional Information: Copyright of this article belongs to Portland Press.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 20 May 2010 09:55
Last Modified: 20 May 2010 09:55
URI: http://eprints.iisc.ac.in/id/eprint/27496

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