Metal ion binding to concanavalin A.
J Biosci
;
1983 Dec; 5(suppl_1): 9-17
Artigo
em Inglês
| IMSEAR
| ID: sea-160269
ABSTRACT
Metal ion activation of saccharide binding has been studied for concanavalin 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+.
Texto completo:
DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Idioma:
Inglês
Revista:
J Biosci
Ano de publicação:
1983
Tipo de documento:
Artigo
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