Srinivas, VR and Reddy, Bhanuprakash G and Surolia, Avadhesa (1999) A predominantly hydrophobic recognition of H-antigenic sugars by winged bean acidic lectin: A thermodynamic study. In: FEBS Letters, 450 (3). pp. 181-185.
PDF
A_predominantly_hydrophobic_recognition.pdf Restricted to Registered users only Download (159kB) | Request a copy |
Abstract
The thermodynamics of binding of winged bean (Psophocarpus tetragonolobus) acidic agglutinin to the H-antigenic oligosaccharide $(Fuc\alpha 1-2Gal \beta 1-4GlcNAc-oMe)$ and its deoxy and methoxy congeners were determined by isothermal titration calorimetry. We report a relatively hydrophobically driven binding of winged bean acidic agglutinin to the congeners of the above sugar. This conclusion is arrived, from the binding parameters of the fucosyl congeners, the nature of the enthalpy-entropy compensation plots and the temperature dependence of binding enthalpies of some of the congeners. Thus, the binding site of winged bean acidic agglutinin must be quite extended to accommodate the trisaccharide, with non-polar loci that recognize the fucosyl moiety of the H-antigenic determinant.
Item Type: | Journal Article |
---|---|
Publication: | FEBS Letters |
Publisher: | Federation of European Biochemical Societies |
Additional Information: | Copyright of this article belongs to Federation of European Biochemical Societies. |
Keywords: | Scanning calorimetry;Congener;Hydrophobicity |
Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
Date Deposited: | 15 Oct 2007 |
Last Modified: | 19 Sep 2010 04:40 |
URI: | http://eprints.iisc.ac.in/id/eprint/12076 |
Actions (login required)
View Item |