Ultizyme International Ltd.

Other

Arkray, Inc.

Bioengineering Laboratories, LLC

Tokyo University of Agriculture and Technology

Techno Medica Co., Ltd.

Roche Diagnostics Operations, Inc.

Lifescan Corporation

I-sens, Inc.

Roche Diabetes Care, Inc.

Roche Diagnostics Gmbh

F. Hoffmann-la Roche Ag

Sode, Koji

Koji Sode

Kazushige Mori

Kazunori Ikebukuro

Wakako Tsugawa

Katsuhiro Kojima

Junko Shimazaki

Yasuhide Kusaka

Hideaki Yamaoka

Hisashi Kaneda

Yuki Ueda

Yosuke Murase

Shido Kawase

Masashi Tsukada

Keisuke Kurosaka

Mitsuhiro Hoshijima

Yuka Takahashi

Masaaki Kurita

Takashi Nishimori

Satoshi Igarashi

Youngjea Kang

Hiroki Yamazaki

Kaori Tsukakoshi

Inyoung Lee

Hideaki c/o Arkray Inc Yamaoka

Mitsuhiro c/o Arkray Inc Hoshijima

Keisuke c/o Unitika Ltd Kurosaka

Shido c/o Unitika Ltd Kawase

The purpose of the present invention is to provide a fungus-derived FADGDH that has a direct electron transfer ability. Provided is a fusion protein comprising a fungus-derived FADGDH or a mutant thereof and a cytochrome molecule connected to the N-terminus of the FADGDH or variant thereof.

Fusion protein of flavin adenine dinucleotide-glucose dehydrogenase and cytochrome molecule

A method for quantifying a target substance, comprising: bringing a sample containing the target substance into contact with a biosensor which comprises an enzyme electrode containing an oxidoreductase and a counter electrode; measuring a change in the potential difference between the enzyme electrode and the counter electrode due to oxidation reaction of the target substance catalyzed by the oxidoreductase; and calculating the concentration of the target substance based on the change in the potential difference; wherein a potential is applied between the enzyme electrode and the counter electrode before the measurement of the change in the potential difference.

Biosensing method

By using a mutant glucose oxidase comprising an amino acid sequence in which a residue corresponding to isoleucine at position 489 or arginine at position 335 in the amino acid sequence of SEQ ID NO:1 is substituted with an amino acid residue having a reactive functional group in a side chain, and binding an electron acceptor to the mutant glucose oxidase through the amino acid residue having a reactive functional group, an electron acceptor-modified glucose oxidase is obtained.

Mutant glucose oxidase and use thereof

A mutant cytochrome protein originated from a cytochrome protein having three heme-binding domains, which mutant cytochrome protein lacks the first heme-binding domain and the second heme-binding domain as counted from the N-terminus, is provided. The mutant cytochrome protein may lack a region(s) containing the first and second heme-binding domains.

Mutant cytochrome protein lacking certain heme domains and use thereof

A molecular recognition element comprising a target molecule-recognizing portion, and a direct electron transfer-type oxidoreductase linked to the target molecule-recognizing portion.

Direct electron transfer-type oxidoreductase-modified molecular recognition element

A method for measuring a glycated protein in a sample, the method comprising (1) a step of allowing a sample in which a degradation product has been generated from a glycated protein by a protease to react with an oxidoreductase in the presence of an electron mediator to generate a reduced electron mediator; and (2) a step of detecting the reaction state in the step (1) by an electrochemical technique using an interdigitated electrode.

Method for measuring glycated protein using interdigitated electrode

Mutant cytochrome protein and use thereof

A measuring method of measuring a concentration of a target ingredient in a sample by using a sensor including an interdigitated array electrode that includes a first electrode and a second electrode, and a reagent layer on the interdigitated array electrode, the measuring method includes: applying a voltage to between the first electrode and the second electrode; measuring a first current value of an electric current flowing between the first electrode and the second electrode; measuring a second current value of the current flowing between the first electrode and the second electrode; calculating the concentration of the target ingredient in the sample, based on a third current value; calculating a correction value, based on the first current value and the second current value; and a step of correcting the concentration of the target ingredient in the sample, based on the correction value.

Measuring method of sensor using interdigitated array electrode, measuring apparatus and computer readable medium storing measuring program

The present invention provides an enzyme electrode composed of a carbon particle on which glucose dehydrogenase (GDH) with flavine adenine dinucleotide (FAD) as a coenzyme is supported and an electrode layer contacting the carbon particle, wherein the carbon particle and/or the electrode layer are/is composed of the carbon particles with a particle diameter of not more than 100 nm and a specific surface area of at least 200 m/g.

Enzyme electrode

Amino acid mutation(s) can be introduced to- or-derived glucose dehydrogenase to obtain a glucose dehydrogenase variant with significantly enhanced productivity in. The glucose dehydrogenase of the present invention is low reactive with xylose.

Glucose dehydrogenase

A modified pyrroloquinoline quinone glucose dehydrogenase that exhibits a high selectivity for glucose is provided. A modified pyrroloquinoline quinone glucose dehydrogenase is disclosed in which the amino acid residue G at Position 99 of a pyrroloquinoline quinone glucose dehydrogenase (PQQGDH) represented by SEQ ID NO: 1, or the amino acid residue G at Position 100 of the pyrroloquinoline quinone glucose dehydrogenase (PQQGDH) represented by SEQ ID NO: 3, is substituted by the amino acid sequence TGZN (where Z is SX, S, or N and X is any amino acid residue). The modified PQQGDH of the present invention may additionally comprise one or more mutations selected from the group consisting of Q192G, Q192A, or Q192S; L193X; E277X; A318X; Y367A, Y367F, or Y367W; G451C; and N452X (where X is any amino acid residue).

A fusion protein of pyrroloquinoline quinone glucose dehydrogenase (PQQGDH) and a cytochrome is disclosed. PQQGDH is, for example, a water-soluble PQQGDH derived from. The cytochrome is, for example, an electron transfer domain of quinohemoprotein ethanol dehydrogenase from. The fusion protein of the present invention shows intramolecular electron transfer from PQQ, a redox center, to the cytochrome, which allow construction of a direct electron transfer-type glucose sensor which requires no electron mediators.

Glucose dehydrogenase/cytochrome fusion protein

An aptamer having a G-quartet structure and being at least one selected from the group consisting of the following polynucleotides, the aptamer having a binding ability to an amyloid protein oligomer: (1) a polynucleotide comprising a base sequence represented by any one of SEQ ID NO:1 to SEQ ID NO:18; (2) a polynucleotide comprising a base sequence that includes at least four sets of at least two consecutive guanosine nucleotides and in which one or several bases has been deleted, substituted, or added in a base sequence represented by any one of SEQ ID NO:18; and (3) a polynucleotide that is a multimer including the polynucleotide of (1) or (2) as a structural unit.

Amyloid protein oligomer-binding aptamer

A glucose dehydrogenase, which is an enzyme that has high substrate specificity, can be produced at a low cost, is not affected by oxygen dissolved in a measurement sample and, in particular, has superior thermal stability is obtained by culturing a microorganism belonging to the genus. A glucose sensor utilizing the glucose dehydrogenase protein is described.

Glucose dehydrogenase and glucose sensor with same

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Tokyo, Japan

Koji Sode