
pmid: 526265
Abstract Co(III) has been stoichiometrically incorporated into jack bean concanavalin A. The Co(III) protein still possesses a binding site for an additional divalent transition metal ion which together with Ca(II) can induce the sugar binding ability. No H2O2 oxidation of Co(II) occurs with demetallized concanavalin A activated with Ca(II) and Co(II) unless Co(II) is present in a stoichiometric excess. Evidence is presented to indicate that kinetically stable Co(III) is bound to a completely different location than the thermodynamically stable Co(II) protein site.
Kinetics, Binding Sites, Nickel, Concanavalin A, Calcium, Cobalt, Protein Binding
Kinetics, Binding Sites, Nickel, Concanavalin A, Calcium, Cobalt, Protein Binding
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