Abstract
Abstract For application in enzyme electrodes liver microsomal cytochrome P-450 was immobilized in a membraneous form. The immobilization yielded 60% of activity and did not impair the functional stability of the enzyme. By coimmobilization of glucose oxidase with P-450 the cofactor NADPH could be replaced by H2O2 formed from the enzymatic glucose oxidation. Fixed to a graphite electrode the obtained preparations were employed for quantitative substrate analysis. The P-450 substrate aniline was measured by anodic oxidation of its hydroqlation product at +250mV. A linear dependence of: the current on aniline concentration up to 0.5mM was obtained.
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