JPWO2009037838A1 - 酵素電極 - Google Patents
酵素電極 Download PDFInfo
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- JPWO2009037838A1 JPWO2009037838A1 JP2009533048A JP2009533048A JPWO2009037838A1 JP WO2009037838 A1 JPWO2009037838 A1 JP WO2009037838A1 JP 2009533048 A JP2009533048 A JP 2009533048A JP 2009533048 A JP2009533048 A JP 2009533048A JP WO2009037838 A1 JPWO2009037838 A1 JP WO2009037838A1
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- 102000004190 Enzymes Human genes 0.000 title claims abstract description 118
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 118
- 239000002245 particle Substances 0.000 claims abstract description 91
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 claims abstract description 76
- 229910052799 carbon Inorganic materials 0.000 claims abstract description 73
- 108010050375 Glucose 1-Dehydrogenase Proteins 0.000 claims abstract description 38
- VWWQXMAJTJZDQX-UYBVJOGSSA-N flavin adenine dinucleotide Chemical compound C1=NC2=C(N)N=CN=C2N1[C@@H]([C@H](O)[C@@H]1O)O[C@@H]1CO[P@](O)(=O)O[P@@](O)(=O)OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C2=NC(=O)NC(=O)C2=NC2=C1C=C(C)C(C)=C2 VWWQXMAJTJZDQX-UYBVJOGSSA-N 0.000 claims abstract description 17
- 235000019162 flavin adenine dinucleotide Nutrition 0.000 claims abstract description 17
- 239000011714 flavin adenine dinucleotide Substances 0.000 claims abstract description 17
- 229940093632 flavin-adenine dinucleotide Drugs 0.000 claims abstract description 17
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- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 claims description 92
- 239000008103 glucose Substances 0.000 claims description 92
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- 241000282320 Panthera leo Species 0.000 description 22
- 229910021607 Silver chloride Inorganic materials 0.000 description 21
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- 238000005259 measurement Methods 0.000 description 12
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- 108090000623 proteins and genes Proteins 0.000 description 8
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- 210000004027 cell Anatomy 0.000 description 7
- 239000007864 aqueous solution Substances 0.000 description 6
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- RXGJTUSBYWCRBK-UHFFFAOYSA-M 5-methylphenazinium methyl sulfate Chemical compound COS([O-])(=O)=O.C1=CC=C2[N+](C)=C(C=CC=C3)C3=NC2=C1 RXGJTUSBYWCRBK-UHFFFAOYSA-M 0.000 description 2
- 241000589513 Burkholderia cepacia Species 0.000 description 2
- 108010052832 Cytochromes Proteins 0.000 description 2
- 102000018832 Cytochromes Human genes 0.000 description 2
- 102100034289 Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 Human genes 0.000 description 2
- 101000641031 Homo sapiens Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 Proteins 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 2
- 239000006230 acetylene black Substances 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
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- 206010033675 panniculitis Diseases 0.000 description 2
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- -1 potassium ferricyanide Chemical compound 0.000 description 2
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- 239000000126 substance Substances 0.000 description 2
- 241001453380 Burkholderia Species 0.000 description 1
- 241000252506 Characiformes Species 0.000 description 1
- 102100025287 Cytochrome b Human genes 0.000 description 1
- 101710205889 Cytochrome b562 Proteins 0.000 description 1
- 108010075028 Cytochromes b Proteins 0.000 description 1
- 101710088194 Dehydrogenase Proteins 0.000 description 1
- 239000012327 Ruthenium complex Substances 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 230000000721 bacterilogical effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000008033 biological extinction Effects 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 150000004696 coordination complex Chemical class 0.000 description 1
- 239000003431 cross linking reagent Substances 0.000 description 1
- 238000006356 dehydrogenation reaction Methods 0.000 description 1
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- 238000005562 fading Methods 0.000 description 1
- KTWOOEGAPBSYNW-UHFFFAOYSA-N ferrocene Chemical compound [Fe+2].C=1C=C[CH-]C=1.C=1C=C[CH-]C=1 KTWOOEGAPBSYNW-UHFFFAOYSA-N 0.000 description 1
- 238000007654 immersion Methods 0.000 description 1
- 230000003100 immobilizing effect Effects 0.000 description 1
- RSAZYXZUJROYKR-UHFFFAOYSA-N indophenol Chemical compound C1=CC(O)=CC=C1N=C1C=CC(=O)C=C1 RSAZYXZUJROYKR-UHFFFAOYSA-N 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
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- 150000002894 organic compounds Chemical class 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
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- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000002689 soil Substances 0.000 description 1
- 238000012289 standard assay Methods 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-N sulfuric acid Substances OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 1
Classifications
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/001—Enzyme electrodes
- C12Q1/005—Enzyme electrodes involving specific analytes or enzymes
- C12Q1/006—Enzyme electrodes involving specific analytes or enzymes for glucose
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/001—Enzyme electrodes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/26—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving oxidoreductase
- C12Q1/32—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving oxidoreductase involving dehydrogenase
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N27/00—Investigating or analysing materials by the use of electric, electrochemical, or magnetic means
- G01N27/26—Investigating or analysing materials by the use of electric, electrochemical, or magnetic means by investigating electrochemical variables; by using electrolysis or electrophoresis
- G01N27/28—Electrolytic cell components
- G01N27/30—Electrodes, e.g. test electrodes; Half-cells
- G01N27/327—Biochemical electrodes, e.g. electrical or mechanical details for in vitro measurements
- G01N27/3271—Amperometric enzyme electrodes for analytes in body fluids, e.g. glucose in blood
- G01N27/3273—Devices therefor, e.g. test element readers, circuitry
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- Organic Chemistry (AREA)
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- Zoology (AREA)
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- Proteomics, Peptides & Aminoacids (AREA)
- Wood Science & Technology (AREA)
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- Immunology (AREA)
- Biochemistry (AREA)
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- General Engineering & Computer Science (AREA)
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- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
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- Genetics & Genomics (AREA)
- Emergency Medicine (AREA)
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- Chemical Kinetics & Catalysis (AREA)
- Hematology (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Apparatus Associated With Microorganisms And Enzymes (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Inert Electrodes (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Abstract
Description
(1)フラビンアデニンジヌクレオチド(FAD)を補酵素とするグルコース脱水素酵素(GDH)が担持された炭素粒子と、前記炭素粒子と接する電極層から構成される酵素電極において、前記炭素粒子及び/又は前記電極層が、粒径100nm以下でかつ比表面積が少なくとも200m2/g以上である炭素粒子から構成されていることを特徴とする酵素電極。
(2)前記グルコース脱水素酵素(GDH)が酸化還元酵素触媒サブユニット又は酸化還元触媒サブユニットと電子伝達サブユニットの複合体である上記(1)に記載の酵素電極。
(3)前記電極層が金属から構成される上記(1)又は(2)に記載の酵素電極。
(4)前記電極層が金属のワイヤーから構成される上記(3)に記載の酵素電極。
(5)グルコースセンサとして使用される上記(1)ないし(4)のいずれかに記載の酵素電極。
(6)フラビンアデニンジヌクレオチド(FAD)を補酵素とするグルコース脱水素酵素(GDH)と、100nm以下でかつ比表面積が少なくとも200m2/g以上である炭素粒子を含むことを特徴とする酵素電極に使用するためのインク材料。
(7)前記グルコース脱水素酵素(GDH)が、酸化還元酵素触媒サブユニット又は酸化還元酵素触媒サブユニットと電子伝達サブユニットの複合体である上記(6)に記載のインク材料。
(8)上記(6)又は(7)に記載のインク材料を、電極層の表面に塗布した後、乾燥させることを特徴とする酵素電極の製造方法。
電極層として炭素粒子を使用する場合の実施例
まず、電極層、酵素層を共に炭素粒子を使用した場合の実施例を示す。
炭素粒子としてKBの代わりに粒径7000 nm、比表面積1m2/gのCPを用いて、実施例1と同様の手順で酵素電極を作成した。すなわち、CP100 mgにミリQ 水400 μl、5 % Nafion(1−プロパノール48%水溶液) 1mlを加えよく混合した後、3日間静置したものをCPインクとし、CPインク10 μlに100 mMp.p.b.(pH 7.0) 10 μl、8.4 U/ml FADGDH 40 μlを混合したものをFADGDH/CPインクとした。KBを電極材料として充填した一体型電極(φ0.4 mm)にFADGDH/CPインクを25 U/mm2となるように滴下し、4 ℃で2時間乾燥させた。作製した酵素電極を作用極、Ptを対極、Ag/AgCl参照電極を参照極とした。3電極方式で、100 mMp.p.b.(pH 7.0) 10 mlを反応溶液とし、+250 mV vs. Ag/AgClの電位を印加した際のグルコース添加に伴う応答電流値を測定した結果を図3に示す。測定は、反応溶液を250 rpmで撹拌し、37 ℃で行った。応答電流値は、各グルコース濃度において測定された電流値からグルコース0 mMにおいて得られた電流値を差し引いたものとした。
炭素粒子としてKBの代わりに粒径7000 nm、比表面積1m2/gのカーボンペースト(以下CP)を用いて、実施例1と同様の手順で酵素電極を作成した。すなわち、CP100 mgにミリQ 水400 μl、5% Nafion(1−プロパノール48%水溶液) 1 mlを加えよく混合した後、3日間静置したものをCPインクとし、CPインク10 μlに100 mM p.p.b.(pH 7.0) 10 μl、8.4 U/ml FADGDH 40 μlを混合したものをFADGDH/CPインクとした。CPを電極材料として充填した一体型電極(φ0.4 mm)にFADGDH/CPインクを25 U/mm2となるように滴下し、4 ℃で2時間乾燥させた。定常になる電流値と反応溶液中のグルコース濃度との相関を図4に示した。図4に示されるように、FADGDH+CP電極の場合は55mMにおける電流値は同じ電極面積、酵素量を用いているにも関わらず55nA程度であった。本酵素電極の5mMグルコースにおける電流密度は330 nA/mm2であった。
次に、電極層として金属ワイヤーを使用し、酵素層としてLPインクを使用した場合の実施例を示す。
Claims (8)
- フラビンアデニンジヌクレオチド(FAD)を補酵素とするグルコース脱水素酵素(GDH)が担持された炭素粒子と、前記炭素粒子と接する電極層から構成される酵素電極において、前記炭素粒子及び/又は前記電極層が、粒径100nm以下でかつ比表面積が少なくとも200m2/g以上である炭素粒子から構成されていることを特徴とする酵素電極。
- 前記グルコース脱水素酵素(GDH)が酸化還元酵素触媒サブユニット又は酸化還元触媒サブユニットと電子伝達サブユニットの複合体である請求項1に記載の酵素電極。
- 前記電極層が金属から構成される請求項1又は2に記載の酵素電極。
- 前記電極層が金属のワイヤーから構成される請求項3に記載の酵素電極。
- グルコースセンサとして使用される請求項1ないし4のいずれかに記載の酵素電極。
- フラビンアデニンジヌクレオチド(FAD)を補酵素とするグルコース脱水素酵素(GDH)と、100nm以下でかつ比表面積が少なくとも200m2/g以上である炭素粒子を含むことを特徴とする酵素電極に使用するためのインク材料。
- 前記グルコース脱水素酵素(GDH)が、酸化還元酵素触媒サブユニット又は酸化還元酵素触媒サブユニットと電子伝達サブユニットの複合体である請求項6に記載のインク材料。
- 請求項6又は7に記載のインク材料を、電極層の表面に塗布した後、乾燥させることを特徴とする酵素電極の製造方法。
Priority Applications (1)
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JP2009533048A JP5273680B2 (ja) | 2007-09-18 | 2008-09-18 | 酵素電極 |
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JP2007240812 | 2007-09-18 | ||
JP2007240812 | 2007-09-18 | ||
JP2008124741 | 2008-05-12 | ||
JP2008124741 | 2008-05-12 | ||
JP2009533048A JP5273680B2 (ja) | 2007-09-18 | 2008-09-18 | 酵素電極 |
PCT/JP2008/002573 WO2009037838A1 (ja) | 2007-09-18 | 2008-09-18 | 酵素電極 |
Publications (2)
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JPWO2009037838A1 true JPWO2009037838A1 (ja) | 2011-01-06 |
JP5273680B2 JP5273680B2 (ja) | 2013-08-28 |
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US (2) | US9617576B2 (ja) |
EP (2) | EP2679990B1 (ja) |
JP (1) | JP5273680B2 (ja) |
CN (2) | CN101802597B (ja) |
CA (1) | CA2699823C (ja) |
ES (2) | ES2555295T3 (ja) |
MX (1) | MX2010002962A (ja) |
RU (1) | RU2476869C2 (ja) |
WO (1) | WO2009037838A1 (ja) |
Families Citing this family (7)
Publication number | Priority date | Publication date | Assignee | Title |
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CN102308204B (zh) | 2009-02-09 | 2014-07-09 | 爱科来株式会社 | 电化学传感器及其制备方法 |
EP2589659B1 (en) | 2009-04-30 | 2015-07-22 | Panasonic Healthcare Holdings Co., Ltd. | Protein-type electron mediator |
CN104583765B (zh) * | 2012-06-25 | 2017-06-06 | 日本生物工程研究所有限责任公司 | 酶电极 |
US10050296B2 (en) | 2013-01-11 | 2018-08-14 | Stc.Unm | Highly efficient enzymatic bioanodes and biocathodes |
ES2484665B2 (es) * | 2013-02-11 | 2015-03-16 | Universidad De Burgos | Dispositivo electródico para la detección de ácido glucónico, procedimiento de fabricación y uso de dicho dispositivo |
JP2021078354A (ja) | 2018-03-08 | 2021-05-27 | 有限会社アルティザイム・インターナショナル | フラビンアデニンジヌクレオチドグルコース脱水素酵素とシトクロム分子との融合タンパク質 |
EP3778476A4 (en) | 2018-03-29 | 2022-03-09 | Toyobo Co., Ltd. | NANOCARBON ELECTRON TRANSFER ACTION |
Citations (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH01503409A (ja) * | 1987-05-01 | 1989-11-16 | ケンブリツジ・ライフ・サイエンシーズ・ピーエルシー | 溶液中の1,4‐ジヒドロニコチンアミドアデニンジヌクレオチド(nadh)の定量のためのアンペア測定的方法 |
JP2003510570A (ja) * | 1999-09-20 | 2003-03-18 | ロシュ ダイアグノスティックス コーポレーション | 連続アナライトモニタリング用小型バイオセンサー |
JP2005502045A (ja) * | 2001-08-28 | 2005-01-20 | デューク・ユニバーシティー | バイオセンサー |
WO2005121355A1 (en) * | 2004-06-04 | 2005-12-22 | Medtronic Minimed, Inc. | Analyte sensors and methods for making and using them |
JP2007509355A (ja) * | 2003-10-24 | 2007-04-12 | バイエル・ヘルスケア・エルエルシー | 酵素的電気化学的バイオセンサ |
WO2007055100A1 (ja) * | 2005-11-08 | 2007-05-18 | Ultizyme International Ltd. | 酵素電極 |
JP2007218795A (ja) * | 2006-02-17 | 2007-08-30 | Toyota Central Res & Dev Lab Inc | 電極材料、並びにそれを用いたバイオセンサー及び燃料電池 |
Family Cites Families (15)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US3669864A (en) * | 1969-09-02 | 1972-06-13 | Robert R Fike | Polarographic electrode apparatus and method |
SE418781B (sv) * | 1977-12-09 | 1981-06-22 | Asea Ab | Sett vid tillverkning av en starkstromskabel |
GB8612861D0 (en) * | 1986-05-27 | 1986-07-02 | Cambridge Life Sciences | Immobilised enzyme biosensors |
GB8817997D0 (en) * | 1988-07-28 | 1988-09-01 | Cambridge Life Sciences | Enzyme electrodes & improvements in manufacture thereof |
US5755953A (en) * | 1995-12-18 | 1998-05-26 | Abbott Laboratories | Interference free biosensor |
US6475372B1 (en) | 2000-02-02 | 2002-11-05 | Lifescan, Inc. | Electrochemical methods and devices for use in the determination of hematocrit corrected analyte concentrations |
JP4721618B2 (ja) * | 2000-09-25 | 2011-07-13 | 旭化成株式会社 | 酵素電極 |
CA2427031C (en) | 2000-10-31 | 2016-02-09 | Koji Sode | Novel glucose dehydrogenase and method for producing the dehydrogenase |
WO2002073181A1 (fr) | 2001-03-13 | 2002-09-19 | Koji Sode | Electrode enzymatique |
JP3862540B2 (ja) | 2001-10-12 | 2006-12-27 | 日本電信電話株式会社 | ナノ金属微粒子含有炭素薄膜電極及びその製造方法 |
US7291256B2 (en) * | 2002-09-12 | 2007-11-06 | Lifescan, Inc. | Mediator stabilized reagent compositions and methods for their use in electrochemical analyte detection assays |
US7638228B2 (en) * | 2002-11-27 | 2009-12-29 | Saint Louis University | Enzyme immobilization for use in biofuel cells and sensors |
US7497940B2 (en) | 2003-09-02 | 2009-03-03 | Koji Sode | Glucose sensor and glucose level measuring apparatus |
JPWO2005093400A1 (ja) * | 2004-03-25 | 2008-02-14 | 有限会社アルティザイム・インターナショナル | 燃料電池型ワイヤレス酵素センサー |
US7955484B2 (en) * | 2005-12-14 | 2011-06-07 | Nova Biomedical Corporation | Glucose biosensor and method |
-
2008
- 2008-09-18 EP EP13186241.9A patent/EP2679990B1/en active Active
- 2008-09-18 ES ES13186241.9T patent/ES2555295T3/es active Active
- 2008-09-18 CN CN200880107747XA patent/CN101802597B/zh active Active
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-
2017
- 2017-02-27 US US15/444,070 patent/US20170191105A1/en not_active Abandoned
Patent Citations (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH01503409A (ja) * | 1987-05-01 | 1989-11-16 | ケンブリツジ・ライフ・サイエンシーズ・ピーエルシー | 溶液中の1,4‐ジヒドロニコチンアミドアデニンジヌクレオチド(nadh)の定量のためのアンペア測定的方法 |
JP2003510570A (ja) * | 1999-09-20 | 2003-03-18 | ロシュ ダイアグノスティックス コーポレーション | 連続アナライトモニタリング用小型バイオセンサー |
JP2005502045A (ja) * | 2001-08-28 | 2005-01-20 | デューク・ユニバーシティー | バイオセンサー |
JP2007509355A (ja) * | 2003-10-24 | 2007-04-12 | バイエル・ヘルスケア・エルエルシー | 酵素的電気化学的バイオセンサ |
WO2005121355A1 (en) * | 2004-06-04 | 2005-12-22 | Medtronic Minimed, Inc. | Analyte sensors and methods for making and using them |
WO2007055100A1 (ja) * | 2005-11-08 | 2007-05-18 | Ultizyme International Ltd. | 酵素電極 |
JP2007218795A (ja) * | 2006-02-17 | 2007-08-30 | Toyota Central Res & Dev Lab Inc | 電極材料、並びにそれを用いたバイオセンサー及び燃料電池 |
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EP2192402B1 (en) | 2013-11-27 |
ES2555295T3 (es) | 2015-12-30 |
CN103472108B (zh) | 2017-09-19 |
EP2192402A1 (en) | 2010-06-02 |
RU2010115275A (ru) | 2011-10-27 |
US20170191105A1 (en) | 2017-07-06 |
US9617576B2 (en) | 2017-04-11 |
JP5273680B2 (ja) | 2013-08-28 |
EP2192402A4 (en) | 2010-09-01 |
ES2441361T3 (es) | 2014-02-04 |
CN101802597B (zh) | 2013-08-21 |
CN103472108A (zh) | 2013-12-25 |
RU2476869C2 (ru) | 2013-02-27 |
MX2010002962A (es) | 2010-03-31 |
EP2679990B1 (en) | 2015-11-04 |
US20100261072A1 (en) | 2010-10-14 |
CA2699823C (en) | 2016-10-25 |
EP2679990A1 (en) | 2014-01-01 |
CA2699823A1 (en) | 2009-03-26 |
CN101802597A (zh) | 2010-08-11 |
WO2009037838A1 (ja) | 2009-03-26 |
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