A bienzyme sensor for the determination of hypoxanthine and inosine
β Scribed by Shengshui Hu; Chung-Chiun Liu
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 526 KB
- Volume
- 9
- Category
- Article
- ISSN
- 1040-0397
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β¦ Synopsis
A biosensor for the detection of hypoxanthine (Hx) and inosine (HxR) has been developed by the coimmobilization of nucleoside phosphorylase ( NP) and xanthine oxidase (XO) on a chemically modified electrode, which uses a glassy carbon electrode coated with a Nafionparaquat film. This sensor responds to Hx and HxR in the presence of phosphate, and it responds only to Hx in the absence of phosphate (borate buffer as medium). The sensor measurement is based on the oxygen consumed due to the enzymatic reaction involving xanthine oxidase which is immobilized on the electrode surface. In this study, the experimental parameters are o timized and the linear relationships between the decreased currents and the concentrations of both Hx and HxR in the range of 1 x 10-6-2 x 10-Mare obtained. This biosensor exhibits a high degree of sensitivity and can be used for the assay for Hx and HxR in fish meat or other biological samples.
π SIMILAR VOLUMES
An enzyme electrode for the successive detection of hypoxanthine and inosine was constructed by co-immobilizing nucleoside phosphorylase and xanthine oxidase on a Nafion-coated platinum disc electrode. The successive responses for hypoxanthine and inosine were obtained in 0.1 M borate buffer (pH 7.5
We describe a sensitive, reproducible method for the simultaneous determination of the ATP catabolites inosine, hypoxanthine, xanthine, and uric acid in biological samples and organ perfusate using reverse-phase chromatography and multiwavelength detection at 254, 270, and 292 nm. Sample preparation
The construction and response of an immobilized enzyme modified electrode as an amperometric sensor is described. Xanthine oxidase was adsorbed on a carbon paste electrode and physically entrapped with a semipermeable membrane. Uric acid, the product of the enzymatic reaction, was oxidized electroc