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Measurement of the Enzyme-CO2-Mg2+ Form of Spinach Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase

Richard E.B. Seftor, James T. Bahr, Richard G. Jensen

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Abstract

When the amount of activation of ribulose 1,5-bisphosphate carboxylase has been measured, two forms of the enzyme, not one, are actually determined experimentally. Only the enzyme-activator CO(2)-Mg(2+) form can bind ribulose bisphosphate for reaction with substrate CO(2) or O(2). A method is presented which measures only this catalytically active form by stabilizing it with ribulose bisphosphate just before dilution and assay in Mg(2+)-free reaction medium.

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When the amount of activation of ribulose 1,5-bisphosphate carboxylase has been measured, two forms of the enzyme, not one, are actually determined experimentally. Only the enzyme-activator CO(2)-Mg(2+) form can bind ribulose bisphosphate for reaction with substrate CO(2) or O(2). A method is presented which measures only this catalytically active form by stabilizing it with ribulose bisphosphate just before dilution and assay in Mg(2+)-free reaction medium.

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Available abstract

When the amount of activation of ribulose 1,5-bisphosphate carboxylase has been measured, two forms of the enzyme, not one, are actually determined experimentally. Only the enzyme-activator CO(2)-Mg(2+) form can bind ribulose bisphosphate for reaction with substrate CO(2) or O(2). A method is presented which measures only this catalytically active form by stabilizing it with ribulose bisphosphate just before dilution and assay in Mg(2+)-free reaction medium.

Key concepts: Ribulose 1,5-bisphosphate, Oxygenase, Pyruvate carboxylase, Spinach, RuBisCO, Enzyme, Chemistry, Ribulose

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