Flow-injection analysis for l -glutamate using immobilized l -glutamate oxidase: comparison of an enzyme reactor and enzyme electrode

Yao, Takeshi; Kobayashi, Naokazu; Wasa, Tamotsu

doi:10.1016/s0003-2670(00)86405-3

Cited by 54 publications

(13 citation statements)

References 9 publications

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“…The calibration plot covered the required concentration ranges of l-glutamate produced by the enzymatic reaction of GOT and GPT. The achieved performance, including the detection limit, was comparable to those of some previously reported l-glutamate sensors using the wild-type enzyme [3,4,6,29].…”

Section: Performance Of the Enzyme In The L-glutamate Sensorsupporting

confidence: 75%

“…The discovery had an enormous impact on the biosensor field. Since then, many amperometric l-glutamate sensors and systems have been developed and used to detect l-glutamate in food samples [3][4][5][6][7] and to reveal the transmitter function of l-glutamate in physiological experiments [8][9][10][11][12][13][14][15][16]. In addition, l-glutamate sensors have been used to analyze the activities of enzymes such as GOT, GPT, and ␥-glutamyl transpeptidase (␥-GTP), which yield l-glutamate as a reaction product [3,[17][18][19][20][21][22].…”

Section: Introductionmentioning

confidence: 99%

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Performance characterization of recombinant l-glutamate oxidase in a micro GOT/GPT sensing system

Upadhyay

Ohgami

Kusakabe

et al. 2006

Sensors and Actuators B: Chemical

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Section: Performance Of the Enzyme In The L-glutamate Sensorsupporting

confidence: 75%

Section: Introductionmentioning

confidence: 99%

Performance characterization of recombinant l-glutamate oxidase in a micro GOT/GPT sensing system

Upadhyay

Ohgami

Kusakabe

et al. 2006

Sensors and Actuators B: Chemical

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“…Various schemes for measuring glutamate based on enzymatic assay have been developed [59][60][61][62][63][64][65][66][67]. With the utilization of glutamate dehydrogenase, coupled with cosubstrate NAD + , the product of the reaction, NADH, can be monitored either by fluorescence or by absorption.…”

confidence: 99%

Selective detection of neurotransmitters by fluorescence and chemiluminescence imaging

Wang

Yeung

2001

Pure and Applied Chemistry

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In recent years, luminescence imaging has been widely employed in neurochemical analysis. It has a number of advantages for the study of neuronal and other biological cells: (1) a particular molecular species or cellular constituent can be selectively visualized in the presence of a large excess of other species in a heterogeneous environment; (2) low concentration detection limits can be achieved because of the inherent sensitivity associated with fluorescence and chemiluminescence; (3) low excitation intensities can be used so that long-term observation can be realized while the viability of the specimen is preserved; and (4) excellent spatial resolution can be obtained with the light microscope so subcellular compartments can be identified. With good sensitivity, temporal and spatial resolution, the flux of ions and molecules and the distribution and dynamics of intracellular species can be measured in real time with specific luminescence probes, substrates, or with native fluorescence. A noninvasive detection scheme based on glutamate dehydrogenase (GDH) enzymatic assay combined with microscopy was developed to measure the glutamate release in cultured cells from the central nervous system (CNS). The enzyme reaction is very specific and sensitive. The detection limit with CCD imaging is down to µM levels of glutamate with reasonable response time. We also found that chemiluminescence associated with the ATP-dependent reaction between luciferase and luciferin can be used to image ATP at levels down to 10 nM in the millisecond time scale. Similar imaging experiments should be feasible in a broad spectrum of biological systems.

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“…As an optimum buffer, 0.1 M phosphate buffer at pH7.5 was selected [9] and pumped with pump A" (Fig. 2).…”

Section: Optimization Of the System For L-ghrtamate Assaymentioning

confidence: 99%

On‐line amperometric assay of glucose, L‐glutamate, and acetylcholine using microdialysis probes and immobilized enzyme reactors

Yao¹,

Suzuki²,

Nishino³

et al. 1995

Electroanalysis

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A highly selective on-line, real-time monitoring system is proposed for amperometric assay of glucose, L-glutamate, and acetylcholine. The system includes a microdialysis probe, immobilized enzyme reactor, and poly( 1,2-diaminobenzene)-coated platinum electrode. The analyte in the dialysate from the microdialysis probe is enzymatically converted to produce hydrogen peroxide. The hydrogen peroxide is detected selectively at a poly(l,2-diaminobenzene)-coated platinum electrode, without any interference from oxidizable species and proteins. The present method can be successfully applied to in vitro assay of glucose and in vivo monitoring of glucose in rat brains. However, the sensitivity is not sufficient for in vivo monitoring of trace amounts of [--glutamate and acetylcholine in rat brains.

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Flow-injection analysis for l -glutamate using immobilized l -glutamate oxidase: comparison of an enzyme reactor and enzyme electrode

Cited by 54 publications

References 9 publications

Performance characterization of recombinant l-glutamate oxidase in a micro GOT/GPT sensing system

Performance characterization of recombinant l-glutamate oxidase in a micro GOT/GPT sensing system

Selective detection of neurotransmitters by fluorescence and chemiluminescence imaging

On‐line amperometric assay of glucose, L‐glutamate, and acetylcholine using microdialysis probes and immobilized enzyme reactors

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