Amperometric Measurement of Creatine Kinase Activity Using an ADP-sensing Bienzyme Electrode

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Abstract
An amperometric ADP-sensing electrode was prepared by immobilizing pyruvate kinase and pyruvate oxidase on an electrode coated with an oxygen-permeable, poly (dimethylsiloxane) layer. The concentration of ADP (2 μM-0.4 mM) could be determined from the decrease in the cathodic current at −0.4 V vs. Ag/AgCl. The bienzyme electrode was applied to the determination of cratine kinase (CK); the enzyme activity (4-1,000 U l-1) was measured from the rate of current decrease, which was caused by the production of ADP through CK-catalyzed reaction.

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