Metal ion binding to concanavalin A |
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Authors: | J. A. Magnuson G. M. Alter D. M. Appel D. J. Christie G. R. Munske E. R. Pandolfino |
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Affiliation: | 1.Biochemistry/Biophysics Program, Department of Chemistry,Washington State University,Pullman,USA |
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Abstract: | Metal ion activation of saccharide binding has been studied for concana-valin A near pH 7.0. Although two metal ions, a transition metal ion and a Ca2+ ion, can bind, both are not required. Ca2+ alone, Mn2+ alone, or Ca2+ with other transition metal ions can activate this lectin. Only one Ca2+ ion per subunit or only one Mn2+ per subunit is sufficient. Metal ion binding was studied by magnetic resonance techniques and direct binding assays. Saccharide binding activity was monitored by following the fluorescence of 4-methylumbelliferyl a-D-mannopyranoside. When Ca2+ binds to demetalized concanavalin A, the transition metal ion site is hindered. When Mn2+ alone binds to demetalized concanavalin A, saccharide binding activity is induced. A subsequent conformational change, not necessary for carbohydrate binding activity, covers the Mn2+. |
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