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Studies on the tryptophan residues of soybean agglutinin. Involvement in saccharide binding

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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.

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Abbreviations

SBA:

soybean agglutinin

NBS:

N-bromosuccinimide

dansyl:

N-dimethyl 5-amino-naphthalene 1-sulphonyl

GalNAc:

N-acetyl D-galactosamine

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Authors and Affiliations

  1. Molecular Biophysics Unit, UGC Centre of Advanced Study, Indian Institute of Science, 560 012, Bangalore, India

    Musti Joginadha Swamy & Avadhesha Surolia

Authors
  1. Musti Joginadha Swamy
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  2. Avadhesha Surolia
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Swamy, M.J., Surolia, A. Studies on the tryptophan residues of soybean agglutinin. Involvement in saccharide binding. Biosci Rep 9, 189–198 (1989). https://doi.org/10.1007/BF01115995

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  • DOI: https://doi.org/10.1007/BF01115995

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