Swamy, Musti Joginadha and Surolia, Avadhesha (1989) Studies on the tryptophan residues of soybean agglutinin. Involvement in saccharide binding. In: Bioscience Reports, 9 (2). pp. 189-198.
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Abstract
Modification of tryptophan side chains of soybean agglutinin (SBA) with N-bromosuccinimide results in a loss of the hemagglutinating and carbohydrate binding activities of the protein. One residue/subunit is probably essential for the binding activity. Modification leads to a large decrease in the fluorescene of the protein accompained by a blue shift. Iodide ion quenching of the protein fluorescence shows that saccharide binding results in a decreased accessibility of some of the tryptophan side chains. These results strongly point towards the involvement of tryptophan residues in the active site of SBA.
Item Type: | Journal Article |
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Publication: | Bioscience Reports |
Publisher: | Springer |
Additional Information: | Copy right of this article belongs to Springer. |
Keywords: | saccharide binding -soybean agglutinin -tryptophan. |
Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
Date Deposited: | 03 Jun 2010 06:47 |
Last Modified: | 19 Sep 2010 06:01 |
URI: | http://eprints.iisc.ac.in/id/eprint/27532 |
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