Mitra, D. ; Sarkar, M. (1989) Physicochemical studies of binding of 4-methylumbelliferyl β-D-galactopyranoside to cold agglutinin Biochemical Journal, 262 (1). pp. 357-360. ISSN 0264-6021
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Official URL: http://www.biochemj.org/content/262/1/357
Related URL: http://dx.doi.org/10.1042/bj2620357
Abstract
The fluorescence of 4-methylumbelliferyl beta-D-galactopyranoside (MeUmbGalp) was quenched in the presence of cold agglutinin, showing that there was binding between MeUmbGalp and cold agglutinin. That binding was saccharide-specific. By using this quenching phenomenon, the association constants (Ka) of the binding of cold agglutinin at different temperatures (10 degrees C and 15 degrees C) to MeUmbGalp and also the number of binding sites were calculated. The Ka values were found to be 2.63 x 10(3) M-1 at 10 degrees C and 1.58 x 10(3) M-1 at 15 degrees C. Though there is a change in Ka values, the number of binding sites was calculated to be six at both temperatures (10 degrees C and 15 degrees C). From the Ka values the thermodynamic parameters (free energy, enthalpy and entropy) of the binding were derived, and analysis of the data indicated that the binding is spontaneous, exothermic and hydrophobic in nature.
Item Type: | Article |
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Source: | Copyright of this article belongs to Portland Press. |
ID Code: | 103330 |
Deposited On: | 05 Feb 2017 16:43 |
Last Modified: | 09 Feb 2017 05:22 |
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