Abstract
An amperometric biosensor, based on an anti-7-hydroxycoumarin (7-OH-coumarin) antibody immobilized at the surface of a glassy carbon electrode, and contained behind a cellulose dialysis membrane, is described. The electrochemical behaviour of this metabolite at the bare glassy carbon electrode was found to be well defined by using differential-pulse voltammetry, and a 90% decrease in peak height was observed on binding of the antibody to the antigen, which occurs at the electroactive site of 7-OH-coumarin. The kinetics of the antibody-antigen reaction was investigated and a first-order reaction was observed with k = 0.0329 mA min-1. This system provides a novel method for studying antibody specificity and the kinetics of such antibody-antigen interactions.
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