Journal
ANALYTICAL SCIENCES
Volume 29, Issue 1, Pages 25-29Publisher
JAPAN SOC ANALYTICAL CHEMISTRY
DOI: 10.2116/analsci.29.25
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An approximate equation for bioelectrocatalitic current was applied to an inhibition reaction analysis of bilirubin oxidase by anion (Cl-, SCN-, and F-) in order to assess the possibility of the electrochemical method for the analysis of enzymatic inhibition reactions. The approximate equation can be transformed into the Michaelis-Menten form, so that the bioelectrocatalitic current can be analyzed by the usual graphical manner, that is, Lineweaver-Burk, Hanes-Woolf, Dixon and Cornish-Bowden plots, if the rate of inhibition reaction is described as a simple Michaelis-Menten form. From the electrochemical assay, it was found that the inhibitor of Cl- and SCN- anions exhibit non-competitive inhibition while that of F- exhibits competitive inhibition, and their inhibition constants were 220, 45, and 22 mM, respectively. The results were essentially similar to those obtained from the conventional spectrophotometric assay.
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