Simultaneous determination of glucose and 1-deoxyglucose in serum by anion-exchange chromatography with an immobilized pyranose oxidase reactor

Kiba, Nobutoshi; Goto, Yuusuke; Furusawa, Motohisa

doi:10.1016/0378-4347(93)80045-6

Cited by 17 publications

(8 citation statements)

References 7 publications

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“…Also, enzyme electrodes have been made with P2O immobilized on membranes for the detection of P2O substrates [26]. P2O from Peniophora gigantea has been used in IMERs for bioprocess monitoring [27] and from Polyporus obtusus for sugar determinations in medical applications [28][29][30][31].…”

Section: Introductionmentioning

confidence: 99%

Pyranose Oxidase Modified Carbon Paste Electrodes for Monosaccharide Determination

et al. 1998

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An amperometric biosensor for the detection of some monosaccharides was developed with co-immobilized pyranose oxidase (purified from the basidiomycete fungus Phanerochaete chrysosporium) and horseradish peroxidase in carbon paste. Due to rather low selectivity of pyranose oxidase, the biosensor could detect both predominating anomers of D-glucose as well as the substrates D-xylose, D-galactose, and d-gluconolactone. The best sensor performance was obtained from a carbon paste with covalently immobilized enzymes together with the additives lactitol and polyethylenimine, resulting in a sensitivity for glucose of 30.2 mA cm ¹2 mM ¹1 . The enzyme modified electrode was investigated in an automated flow injection system at the operating potential of ¹50 mV (vs. Ag/AgCl) with an injection frequency of 40 h ¹1 . The biosensor was also integrated as the detection unit in a liquid chromatographic system for the detection of monosaccharides to show its potential use in real applications.

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Section: Introductionmentioning

confidence: 99%

Pyranose Oxidase Modified Carbon Paste Electrodes for Monosaccharide Determination

et al. 1998

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“…12,13) Another biological function is thought to be the production of D-glucosone (D-arabino-hexos-2-ulose) as a precursor of an antibiotic, cortalcerone, the production of which is widely (but not wholly) distributed among white-rot fungi. 14,15) Pyranose oxidase has a signiˆcant application to the quantitative analysis of D-glucose in blood 5,16) and glucose biosensors, 17) with an advantage over glucose oxidase in that this enzyme reacts to both the a-and b-anomers of D-glucose. This enzyme is also expected to be useful as a diagnostic enzyme because it reacts with 1,5-anhydro-D-glucitol, a diagnostic marker of diabetes mellitus.…”

mentioning

confidence: 99%

Purification, Characterization, and Molecular Cloning of a Pyranose Oxidase from the Fruit Body of the Basidiomycete,Tricholoma matsutake

Takakura

Kuwata

2003

Bioscience, Biotechnology, and Biochemistry

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A new H(2)O(2)-generating pyranose oxidase was purified as a strong antifungal protein from an arbuscular mycorrhizal fungus, Tricholoma matsutake. The protein showed a molecular mass of 250 kDa in gel filtration, and probably consisted of four identical 62 kDa subunits. The protein contained flavin moiety and it oxidized D-glucose at position C-2. H(2)O(2) and D-glucosone produced by the pyranose oxidase reaction showed antifungal activity, suggesting these compounds were the molecular basis of the antifungal property. The V(max), K(m), and k(cat) for D-glucose were calculated to be 26.6 U/mg protein, 1.28 mM, and 111/s, respectively. The enzyme was optimally active at pH 7.5 to 8.0 and at 50 degrees C. The preferred substrate was D-glucose, but 1,5-anhydro-D-glucitol, L-sorbose, and D-xylose were also oxidized at a moderate level. The cDNA encodes a protein consisting of 564 amino acids, showing 35.1% identity to Coriolus versicolor pyranose oxidase. The recombinant protein was used for raising the antibody.

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“…1,2) IMERs have been used to study the enzymatic enantioselective recognition of racemic compounds 3) and the on-line synthesis and analysis of drug metabolites. 4,5) We have also previously prepared immobilized enzyme phospholipid columns with biomimetic characteristics for HPLC columns and examined their properties as enzyme reactors and their usage for drug development.…”

Section: Notesmentioning

confidence: 99%

Development of a Rapid and Detailed Structural Identification System with an On-Line Immobilized Enzyme Reactor Integrated into LC-NMR

Kashima

Okabayashi

2010

CHEMICAL & PHARMACEUTICAL BULLETIN

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Immobilized enzyme reactors (IMERs) integrated into an LC-NMR system were developed for rapid and detailed structural identification of enzymatic reaction products. An on-column enzymatic reaction was achieved for immobilized cytochrome-c and dog microsomes. After the reaction, these products were analyzed by LC-NMR without any work-up processes. The immobilized cytochrome-c column integrated into LC-NMR was used to characterize the reaction product formed on N-demethylation by measurement of

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Simultaneous determination of glucose and 1-deoxyglucose in serum by anion-exchange chromatography with an immobilized pyranose oxidase reactor

Cited by 17 publications

References 7 publications

Pyranose Oxidase Modified Carbon Paste Electrodes for Monosaccharide Determination

Pyranose Oxidase Modified Carbon Paste Electrodes for Monosaccharide Determination

Purification, Characterization, and Molecular Cloning of a Pyranose Oxidase from the Fruit Body of the Basidiomycete,Tricholoma matsutake

Development of a Rapid and Detailed Structural Identification System with an On-Line Immobilized Enzyme Reactor Integrated into LC-NMR

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