Studies on the tryptophan residues of soybean agglutinin. Involvement in saccharide binding |
| |
Authors: | Musti Joginadha Swamy Avadhesha Surolia |
| |
Affiliation: | (1) Molecular Biophysics Unit, UGC Centre of Advanced Study, Indian Institute of Science, 560 012 Bangalore, India |
| |
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.Abbreviations SBA soybean agglutinin - NBS N-bromosuccinimide - dansyl N-dimethyl 5-amino-naphthalene 1-sulphonyl - GalNAc N-acetyl D-galactosamine |
| |
Keywords: | saccharide binding soybean agglutinin tryptophan |
本文献已被 SpringerLink 等数据库收录! |