Determination of glutamate pyruvate transaminase and pyruvate with an amperometric pyruvate oxidase sensor

Mizutani, Fumio; Tsuda, Keishiro; Karube, Isao; Suzuki, Shuichi; Matsumoto, Kunio

doi:10.1016/s0003-2670(01)93714-6

Cited by 55 publications

(18 citation statements)

References 7 publications

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“…Covalent attachment on the surface of electrodeposited polytyramine EDC and NHS or Glutaraldehyde (À) Electrochemical entrapment throughout polytyramine followed by covalent attachment EDC and NHS (À) Electrochemical entrapment of enzyme throughout polytyramine Without covalent attachment (À) SAM using thiol EDC and NHS (À) Covalent attachment onto the surface of polytyramine in humid conditions EDC or Glutaraldehyde () The concentrations of cofactors used to measure pyruvate in this study (2 mM TPP, 2 mM FAD and 1 mM MgCl 2 ) were consistent with previous reports for entrapped pyruvate oxidase [14,15,37]. The optimal pH in a buffer of 0.01 M Trizma and 0.04 M phosphate was found to be 7.2 in common with other studies [14,15].…”

Section: Enzyme Immobilization Methods Crosslinking Agents Resultssupporting

confidence: 87%

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The Development of a Pyruvate Biosensor Using Electrodeposited Polytyramine

et al. 2002

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Section: Enzyme Immobilization Methods Crosslinking Agents Resultssupporting

confidence: 87%

“…The optimal pH in a buffer of 0.01 M Trizma and 0.04 M phosphate was found to be 7.2 in common with other studies [14,15].…”

Section: Enzyme Immobilization Methods Crosslinking Agents Resultssupporting

confidence: 84%

The Development of a Pyruvate Biosensor Using Electrodeposited Polytyramine

et al. 2002

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“…The pH optimum for soluble and immobilized pyruvate oxidases were reported to be 7.0. 8 The color intensity of the indicator reaction using MBTH-DMA-peroxidase did not change over a pH range of 5-8. Therefore, pH 7.0 was selected for optimal enzyme reaction and maximal color intensity.…”

Section: Properties Of Immobilized Pyruvate Oxidase Columnmentioning

confidence: 91%

Determination of inorganic phosphorus using immobilized pyruvate oxidase

Tabata

Murachi

1983

Biotech & Bioengineering

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A new method for the automated analysis of inorganic phosphorus using immobilized enzyme was established. The method was based on the determination of hydrogen peroxide formed by the action of pyruvate oxidase on inorganic phosphate and pyruvate. Since pyruvate oxidase required inorganic phosphate for its stability and therefore had to be kept in a buffer containing inorganic phosphate, it could hardly be used as a reagent in the form of aqueous solution for the determination of inorganic phosphorus. This difficulty was overcome by using immobilized pyruvate oxidase in column form. When the present method was applied to the determination of inorganic phosphorus in serum, it gave perfect linearity of the data up to 0.20 g inorganic phosphorus/L with satisfactory precision, reproducibility, high sensitivity, and accurate recoveries. The immobilized enzyme reactor unit showed enhanced heat stability and good operational stability for a one-month period, during which time it was used over 900 times for analyses. The enzyme column was not affected by organic phosphorus compounds. The results correlated satisfactorily with those obtained by another well-established method.

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“…Amperometric enzyme electrodes, in partiicular, have been studied because of their potential for (a high detection sensitivity and capability for analyzing colored or turbid solutions with inexpensive instrumentation [ I , 21. Significant attention has been focused on oxidase enzymes for the development of enzyme electrodes, and sensors have been developed for a variety of analytes including glucose [3], oxalate [4] and pyruvate [5]. In addition, amperometric immunoassays have been reported employing enzyme labels such as alkaline phosphatase and glucose oxidase [6, 71 capable of generating an electrochemically active product.…”

Section: Introductionmentioning

confidence: 99%

Mediated amperometric detection of glucose-6-phosphate dehydrogenase at a poly(vinyl chloride) covered electrode using 1,4-benzoquinone and diaphorase

et al. 1995

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Reduced nicotinamide adenine dinucleotide (NADH), produced from glucose-6-phosphate dehydrogenase (G6PDH) was catalytically oxidized using diaphorase and 1,4-benzoquinone to yield 1,4-hydroquinone. This benzoquinone redox mediator was readily detected at an electrode polarized at +0.5 V (vs. Ag/AgCI) so avoiding the high overpotentials required for a direct electrochemical measurement of NADH. Also, the lipophilic nature of the hydroquinone enabled a novel high selectivity plasticized PVC membrane mounted over the electrode to be exploited. The mediator/PVC combination achieved NADH calibration linear up to at least 1 0 0~~. When used to assay G6PDH activity, a linear calibration from 0.1-1.0 U/mL was produced. The detection system offers the possibility of highly selective measurement of dehydrogenase enzyme activity in biological samples without sample preparation and could provide the basis for simplified homogeneous immunoassays as well as dehydrogenase amperometric enzyme electrodes.

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Determination of glutamate pyruvate transaminase and pyruvate with an amperometric pyruvate oxidase sensor

Cited by 55 publications

References 7 publications

The Development of a Pyruvate Biosensor Using Electrodeposited Polytyramine

The Development of a Pyruvate Biosensor Using Electrodeposited Polytyramine

Determination of inorganic phosphorus using immobilized pyruvate oxidase

Mediated amperometric detection of glucose-6-phosphate dehydrogenase at a poly(vinyl chloride) covered electrode using 1,4-benzoquinone and diaphorase

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