A Co(III) derivative of concanavalin A

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 H 2O 2 oxidation of Co(II) occurs with demetallized c...

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Veröffentlicht in:Biochemical and biophysical research communications 1979-12, Vol.91 (3), p.1045-1050
Hauptverfasser: Urdea, M.S., Christie, D.J., Munske, G.R., Magnuson, J.A., Legg, J.I.
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container_end_page 1050
container_issue 3
container_start_page 1045
container_title Biochemical and biophysical research communications
container_volume 91
creator Urdea, M.S.
Christie, D.J.
Munske, G.R.
Magnuson, J.A.
Legg, J.I.
description 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 H 2O 2 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.
doi_str_mv 10.1016/0006-291X(79)91985-5
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subjects Binding Sites
Calcium
Cobalt
Concanavalin A
Kinetics
Nickel
Protein Binding
title A Co(III) derivative of concanavalin A
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