Stabilization of the Substrate Reaction of Horseradish Peroxidase with o-Phenylenediamine in the Enzyme Immunoassay

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Abstract
When the horseradish peroxidase reaction is stopped with acid, the decay of unconverted hydrogen peroxide is responsible for the further oxidation of o-phenylenediamine. This leads to a time-dependent flattening of the standard curve in the enzyme immunoassay, after the reaction was stopped. Addition of reducing agents, such as sulfite ions, to the stopping solution, prevents the further oxidation of o-phenylenediamine by completely reducing the remaining hydrogen peroxide. The developed color is then stabilized.

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