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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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|
|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|
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