JPS62228274A - Thin membrane of immobilized enzyme - Google Patents
Thin membrane of immobilized enzymeInfo
- Publication number
- JPS62228274A JPS62228274A JP61070362A JP7036286A JPS62228274A JP S62228274 A JPS62228274 A JP S62228274A JP 61070362 A JP61070362 A JP 61070362A JP 7036286 A JP7036286 A JP 7036286A JP S62228274 A JPS62228274 A JP S62228274A
- Authority
- JP
- Japan
- Prior art keywords
- glucose oxidase
- electrode
- immobilized enzyme
- aniline
- thin film
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- 108010093096 Immobilized Enzymes Proteins 0.000 title claims description 15
- 239000012528 membrane Substances 0.000 title abstract description 7
- 108010015776 Glucose oxidase Proteins 0.000 claims abstract description 14
- 239000004366 Glucose oxidase Substances 0.000 claims abstract description 14
- 229940116332 glucose oxidase Drugs 0.000 claims abstract description 14
- 235000019420 glucose oxidase Nutrition 0.000 claims abstract description 14
- PAYRUJLWNCNPSJ-UHFFFAOYSA-N N-phenyl amine Natural products NC1=CC=CC=C1 PAYRUJLWNCNPSJ-UHFFFAOYSA-N 0.000 claims abstract description 13
- 229920000642 polymer Polymers 0.000 claims abstract description 4
- 239000010409 thin film Substances 0.000 claims description 14
- BASFCYQUMIYNBI-UHFFFAOYSA-N platinum Chemical compound [Pt] BASFCYQUMIYNBI-UHFFFAOYSA-N 0.000 abstract description 18
- 230000000694 effects Effects 0.000 abstract description 9
- 229910052697 platinum Inorganic materials 0.000 abstract description 9
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 abstract description 7
- 239000001301 oxygen Substances 0.000 abstract description 7
- 229910052760 oxygen Inorganic materials 0.000 abstract description 7
- 238000006116 polymerization reaction Methods 0.000 abstract description 7
- 230000035699 permeability Effects 0.000 abstract description 6
- 239000011521 glass Substances 0.000 abstract description 4
- 229920000767 polyaniline Polymers 0.000 abstract description 4
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 abstract description 3
- -1 aniline compound Chemical class 0.000 abstract description 3
- 229910021607 Silver chloride Inorganic materials 0.000 abstract 1
- 239000008280 blood Substances 0.000 abstract 1
- 210000004369 blood Anatomy 0.000 abstract 1
- HKZLPVFGJNLROG-UHFFFAOYSA-M silver monochloride Chemical compound [Cl-].[Ag+] HKZLPVFGJNLROG-UHFFFAOYSA-M 0.000 abstract 1
- 235000011149 sulphuric acid Nutrition 0.000 abstract 1
- 102000004190 Enzymes Human genes 0.000 description 10
- 108090000790 Enzymes Proteins 0.000 description 10
- 229940088598 enzyme Drugs 0.000 description 10
- 238000000034 method Methods 0.000 description 10
- 150000001448 anilines Chemical class 0.000 description 6
- 239000010408 film Substances 0.000 description 5
- RGHNJXZEOKUKBD-SQOUGZDYSA-N D-gluconic acid Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(O)=O RGHNJXZEOKUKBD-SQOUGZDYSA-N 0.000 description 3
- AFBPFSWMIHJQDM-UHFFFAOYSA-N N-methyl-N-phenylamine Natural products CNC1=CC=CC=C1 AFBPFSWMIHJQDM-UHFFFAOYSA-N 0.000 description 3
- 102000003992 Peroxidases Human genes 0.000 description 3
- 108040007629 peroxidase activity proteins Proteins 0.000 description 3
- RGHNJXZEOKUKBD-UHFFFAOYSA-N D-gluconic acid Natural products OCC(O)C(O)C(O)C(O)C(O)=O RGHNJXZEOKUKBD-UHFFFAOYSA-N 0.000 description 2
- 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 description 2
- OJGMBLNIHDZDGS-UHFFFAOYSA-N N-Ethylaniline Chemical compound CCNC1=CC=CC=C1 OJGMBLNIHDZDGS-UHFFFAOYSA-N 0.000 description 2
- 125000000217 alkyl group Chemical group 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 239000003792 electrolyte Substances 0.000 description 2
- 125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 description 2
- 229950006191 gluconic acid Drugs 0.000 description 2
- 235000012208 gluconic acid Nutrition 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 2
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 2
- RZXMPPFPUUCRFN-UHFFFAOYSA-N p-toluidine Chemical compound CC1=CC=C(N)C=C1 RZXMPPFPUUCRFN-UHFFFAOYSA-N 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 229920000128 polypyrrole Polymers 0.000 description 2
- 238000001228 spectrum Methods 0.000 description 2
- HLBLWEWZXPIGSM-UHFFFAOYSA-N 4-Aminophenyl ether Chemical compound C1=CC(N)=CC=C1OC1=CC=C(N)C=C1 HLBLWEWZXPIGSM-UHFFFAOYSA-N 0.000 description 1
- 229910001369 Brass Inorganic materials 0.000 description 1
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 1
- 241000283986 Lepus Species 0.000 description 1
- UEZVMMHDMIWARA-UHFFFAOYSA-N Metaphosphoric acid Chemical compound OP(=O)=O UEZVMMHDMIWARA-UHFFFAOYSA-N 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 1
- 241000270295 Serpentes Species 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000005273 aeration Methods 0.000 description 1
- 125000003545 alkoxy group Chemical group 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 125000004104 aryloxy group Chemical group 0.000 description 1
- 239000010951 brass Substances 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 229910001882 dioxygen Inorganic materials 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 125000001301 ethoxy group Chemical group [H]C([H])([H])C([H])([H])O* 0.000 description 1
- 239000000174 gluconic acid Substances 0.000 description 1
- 125000000623 heterocyclic group Chemical group 0.000 description 1
- 230000003100 immobilizing effect Effects 0.000 description 1
- 125000000956 methoxy group Chemical group [H]C([H])([H])O* 0.000 description 1
- 239000011259 mixed solution Substances 0.000 description 1
- 210000001819 pancreatic juice Anatomy 0.000 description 1
- 125000000951 phenoxy group Chemical group [H]C1=C([H])C([H])=C(O*)C([H])=C1[H] 0.000 description 1
- 230000000379 polymerizing effect Effects 0.000 description 1
- 239000012047 saturated solution Substances 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 125000002023 trifluoromethyl group Chemical group FC(F)(F)* 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Abstract
Description
【発明の詳細な説明】
（産業上の利用分野）
本発明は固定化酵素薄膜に係り、更に具体的Ｋｕ、グル
コースオキシダーゼの酵素活性を保持したアニリン■の
重合体からなる固定化酵素薄膜に関する。DETAILED DESCRIPTION OF THE INVENTION (Field of Industrial Application) The present invention relates to an immobilized enzyme thin film, and more specifically to an immobilized enzyme thin film made of a polymer of Ku and aniline (2) that retains the enzymatic activity of glucose oxidase.
（従来の技術）
従来、酵素の固定化方法としては、包括法、架橋化法、
共有結合法等が知られている。更に最近、固定化酵素薄
膜として、例えば゛屯気化学道合法によシ、グルコース
オキシダーゼ・ポリピロール導電性酵素薄膜が作られた
・ところがこのようなポリピロール酵素薄膜は、その導
電性ゆえ、電極被覆膜として使用する場合、選択性に劣
るという欠点があった。すなわち、＃素活性を発現させ
る設定電位において、ポリピロール酵素薄膜で棟々の分
子が反応を起こすという問題点がめった。(Conventional technology) Conventionally, enzyme immobilization methods include entrapment method, crosslinking method,
Covalent bonding methods and the like are known. Furthermore, recently, as an immobilized enzyme thin film, for example, a glucose oxidase/polypyrrole conductive enzyme thin film has been made using the ``Tun Kagakudo method''. When used as a membrane, it had the disadvantage of poor selectivity. In other words, at the set potential that causes the #primary activity to be expressed, a problem has arisen in which various molecules in the polypyrrole enzyme thin film often react.
（発明の目的）
本発明の目的は、選択性に優れ、かつ簡便で強固な固定
化酵素薄膜を提供することにある。(Object of the Invention) An object of the present invention is to provide a simple and strong immobilized enzyme thin film with excellent selectivity.
また、酸素透過性の優れた固定化酵素Ｈ膜を提供するこ
とにある。Another object of the present invention is to provide an immobilized enzyme H membrane with excellent oxygen permeability.
（発明の構成・）
本発明の目的は、グルコースオキシダーゼを有するアニ
リン類の重合体からなる固定化酵素薄Ｂｍによって達成
される。(Structure of the Invention) The object of the present invention is achieved by an immobilized enzyme thin Bm made of a polymer of anilines having glucose oxidase.
以下詳細に本発明を説明する。The present invention will be explained in detail below.
まず、本発明に係るアニリン類としては、例えば一般式
（１）で表わされるものが挙げられる。First, examples of the anilines according to the present invention include those represented by general formula (1).
人雪
上記式中、Ｒ＋、Ｒｓは水素原子またはメチル基、エチ
ル基等のアルキル基を表わし、Ｘ＋、Ｌは水素原子、ア
ミン基、メチル基、エチル基等のアルキル基、メトキシ
基、エトキシ基等のアルコキシル基、フェノキシ基、ア
ミノフェノキシ基等のアリールオキシ基、カルボキシル
基、トリフルオロメチル基等のフッ素置換アルキル基を
表わし、また、Ｘ８、Ｘ、は芳香環又は複素環を形成し
ていてもよい。更に具体的には、一般式（１）で表わさ
れるアニリン類として、アニリン、〇−フェニレンジア
ミン、ｐ−トルイジン、リーメトキシアニリン、コ、６
−シメチルアニリン１．２．ｊ−ジメトキシアニリン、
Ｎ−メチルアニリン、Ｎ−エチルアニリン、ダ謎′−ジ
アミノジフェニルエーテル、ダーアミノ安息査Ｍ、−２
−１リフルオロメチルアニリン、ｊ−アミノ−／、 ／
０−フェナントロリン等が例示できる。In the above formula, R+ and Rs represent a hydrogen atom or an alkyl group such as a methyl group or an ethyl group, and X+ and L represent a hydrogen atom, an alkyl group such as an amine group, a methyl group, or an ethyl group, a methoxy group, or an ethoxy group. represents an alkoxyl group such as a phenoxy group, an aryloxy group such as an aminophenoxy group, a carboxyl group, a fluorine-substituted alkyl group such as a trifluoromethyl group, and X8 and X form an aromatic ring or a heterocyclic ring. Good too. More specifically, the anilines represented by the general formula (1) include aniline, 〇-phenylenediamine, p-toluidine, riemethoxyaniline,
-dimethylaniline 1.2. j-dimethoxyaniline,
N-methylaniline, N-ethylaniline, diaminodiphenyl ether, diaminobencho M, -2
-1 Lifluoromethylaniline, j-amino-/, /
Examples include 0-phenanthroline.
本発明で使用するグルコースオキシダーゼは、グルコー
スを酸化してＤ−グルコン酸を生ずる反応を触媒する公
知の酵素である。Glucose oxidase used in the present invention is a known enzyme that catalyzes a reaction that oxidizes glucose to produce D-gluconic acid.
本発明の固定化酵素薄膜は、上ａピのアニリン類とグル
コースオキシダーゼを、電気化学重合法などの常法を用
いて固定化すること釦より製造される。The immobilized enzyme thin film of the present invention is produced by immobilizing the above anilines and glucose oxidase using a conventional method such as electrochemical polymerization.
すなわち、例えば、電）膵液中にアニリン類およびグル
コースオキシダーゼを加え、ｈ！１−ｔＪｃｌ 電極を
参照電極とした電解セル内において、定電位あるいは定
電流電気化学重合法により、一定温度で行なわれる。こ
こで使用される電解液に制限はなく、例えばθ、／ ｍ
Ｍ以上の硫酸あるいは適当濃度のリン酸緩衝液等が選ば
れるが、酸性度が上がるほど固定化酵素薄膜の酵素活性
は良くなる傾向にある。ま九、アニリン類およびグルコ
ースオキシダーゼの濃度はそれぞれ例えば、２３７ｒＬ
Ｍ〜／Ｍおよび０． ／ ｍｅ） ／ ｍｅ 〜ｊ Ｏ
ｍｙ／ ｍｌの範囲が適当である。更に、電解セルおよ
び作用極・対極に制限はなく、それぞれ例えばガラスセ
ルおよび白金電極等が使用できる。定電位で重合する場
合、良質な膜を得るため設定電位は０．Ｊ Ｖ ｖｓ
Ａｌｌ・Ａ１０１１以上であることが望ましい。That is, for example, by adding anilines and glucose oxidase to pancreatic juice, h! The process is carried out at a constant temperature by constant potential or constant current electrochemical polymerization in an electrolytic cell using a 1-tJcl electrode as a reference electrode. There is no limit to the electrolyte used here, for example θ,/m
Sulfuric acid with a concentration of M or higher or a phosphate buffer with an appropriate concentration is selected, and the enzyme activity of the immobilized enzyme thin film tends to improve as the acidity increases. For example, the concentration of anilines and glucose oxidase is 237 rL, respectively.
M~/M and 0. / me) / me ~j O
A range of my/ml is appropriate. Furthermore, there are no restrictions on the electrolytic cell and the working and counter electrodes, and for example, glass cells and platinum electrodes can be used, respectively. When polymerizing at a constant potential, the set potential is set to 0.0 to obtain a good quality film. JV vs.
It is preferable that All.A1011 or higher.
−また、重合温度は、例えば通常ｓ ’Ｃ〜Ｓθ℃の間
から選ばれる。-Also, the polymerization temperature is usually selected, for example, from s'C to SθC.
このようにして得られる固定化酵素薄膜は、選択性の高
い酵素活性を有し、更に酵素膜は電極表面に強固に付着
して容易にはがれず、酸素透過性も良い。The immobilized enzyme thin film obtained in this manner has highly selective enzyme activity, and furthermore, the enzyme film firmly adheres to the electrode surface and does not easily peel off, and has good oxygen permeability.
（実施例）
以下に実施例を示し、本発明の固定化酵素薄膜について
更に詳細に説明するが、本発明はその要旨を越えない限
り以下の実施例に限定されるものではない。(Example) The immobilized enzyme thin film of the present invention will be explained in more detail by referring to Examples below, but the present invention is not limited to the following Examples unless the gist thereof is exceeded.
実施例／
実験装置の概略を図／に示す。白金電極を作用極および
対極とし、ＡＪ’−Ａ、ＨＡ！電極を参照電極としたガ
ラス製電解セルを用い、０．／Ｍアニリントクルコース
オキシダーゼ１０■を含ｂＯ，／Ｍ Ｈｅ Ｓｏ４溶液
−Ｍ中で、一定温度、において、７．２θ秒間、０．９
Ｖ（対ｈＥ−ｈ９０１１ ）の定電位をかけて電気化学
重合を行なった。Example/ A schematic of the experimental apparatus is shown in Figure/. Using platinum electrodes as working and counter electrodes, AJ'-A, HA! Using a glass electrolytic cell with the electrode as a reference electrode, 0. /M anilinetocurose oxidase 10μ in bO, /M He So4 solution-M at constant temperature for 7.2θ seconds, 0.9
Electrochemical polymerization was performed by applying a constant potential of V (vs. hE-h9011).
この時、白金電極表面は薄縁色に変色した。終了後、白
金電極表面に酵素固定化ポリアニリン膜が生成され、か
つ酵素活性が保持されていることを確かめるために、ペ
ルオキシダーゼ法を採用した。すなわち、！＠を洗浄後
乾燥し、７Ｍグ／Ｌ−ニア −ス０．Ｊ ａｔ、 ０．
／ Ｍフェノール０．．１ａｔ、 ０．／ Ｍ 弘−ア
ミノアンチピリン０．３ｒｎｅ。At this time, the surface of the platinum electrode changed color to a faint color. After completion, a peroxidase method was employed to confirm that an enzyme-immobilized polyaniline film was produced on the surface of the platinum electrode and that enzyme activity was maintained. In other words! After washing and drying, 7Mg/L-Nia-su0. J at, 0.
/M phenol 0. ．． 1at, 0. /M Hiro-aminoantipyrine 0.3rne.
０．３１す／属ペルオキシダーゼ０．３ｍｌおよび０．
７Ｍ ＩＪン酸Ｍ衝液／、ざｍｌの混合溶液中に浸漬し
た。0.31 ml/genus peroxidase and 0.3 ml.
It was immersed in a mixed solution of 7M IJ acid M solution/1ml.
約ｌＳ分間放置した後、３０３ ｎｍの可視光スペクト
ルを測定した。可視光スペクトルの吸光ｔから、グルコ
ースオキシダーゼの酵素活性量を求めると、２７ Ａ
ｎｊｌ／ｃｎｉであった。After leaving it for about 1S minutes, the visible light spectrum at 303 nm was measured. The amount of enzyme activity of glucose oxidase is determined from the absorption t of the visible light spectrum, 27 A
It was njl/cni.
尚、ポリアニリン膜の酸素透過性を調べるため、前述の
方法においてアニＩＪンのみを使用して白金電極表面に
ポリアニリン膜を生成させ、これをθ、／Ｍリン酸ｉ衝
液中、Ｏ〜−〇、６Ｖ（対Ａ１１ｌＡ＆Ｏ１，）の電位
域で常法に従い電位走査を行ったところ、第一図に示す
ように、酸素ガスの通気により還元電流は大きく増大し
、膜中を酸素が透過し、白金電極上で電気化学還元され
ることが分った。In order to examine the oxygen permeability of the polyaniline film, a polyaniline film was formed on the surface of the platinum electrode using only aniline in the method described above, and this was heated in θ, /M phosphoric acid buffer solution from O to −〇. , 6V (vs. A11lA&O1,) potential scanning was carried out according to a conventional method in the potential range.As shown in Figure 1, the reduction current greatly increased due to the aeration of oxygen gas, oxygen permeated through the membrane, and the platinum It was found that electrochemical reduction occurred on the electrode.
実施例コ
０．１Ｍリン酸緩衝液２ ａｔに、０．１Ｍアニリンお
よびグルコースオキシダーゼデ、デ〜を溶かし、実施例
／と同様な方法で電気化学重合を行なった。この時、白
金電極表面は薄黄銅色となった。Example 0.1M aniline and glucose oxidase were dissolved in 2 atM of 0.1M phosphate buffer, and electrochemical polymerization was carried out in the same manner as in Example. At this time, the surface of the platinum electrode became a light brass color.
終了後、ペルオキシダーゼ法によりグルコースオキシダ
ーゼの活性量を求めると、１ｌｊｎｌ／ｃｒｔｌであっ
た。After completion, the activity of glucose oxidase was determined by the peroxidase method and was found to be 1ljnl/crtl.
（発明の効果）
本発明によれば、酵素活性を保持し、選択性が高く、更
に酸素透過性が良い強固な固定化酵素薄膜が得られる。(Effects of the Invention) According to the present invention, a strong immobilized enzyme thin film that retains enzyme activity, has high selectivity, and has good oxygen permeability can be obtained.
本発明の固定化酵素薄膜はバイオセンサーや、臨床検査
用のグルコース検出装置、あるいはグルコン酸生成のバ
イオリアクター等への応用が可能である。The immobilized enzyme thin film of the present invention can be applied to biosensors, glucose detection devices for clinical testing, bioreactors for producing gluconic acid, and the like.
更に、電気化学重合法などを用いれば、微小な電極の表
面に容易に固定化酵素薄膜を作製できるため、ミクロな
パターンを有したノくイオ素子図／は、実施例で吠用し
た電解装置の概略図を示す。Furthermore, if an electrochemical polymerization method is used, an immobilized enzyme thin film can be easily produced on the surface of a microelectrode. A schematic diagram is shown.
図ユは、実施例／で製造したボリアニＩＪン膜の酸素透
過性を示す。Figure 1 shows the oxygen permeability of the Borian IJ membrane produced in Example/.
■ 作用極 ■対極 （り参照極 ■塩橋 （５）ガラス製電解セル Ω 電解液 ■ ＫＯ１飽和溶液 出 願 人 三菱化成工業株式会社 代 理 人 弁理士 長谷用 − （ほか７名） 図 １ 巳２ 電路立Ｖ（対Ａｙ／ＡｇＣ１）■ Working electrode ■Opposite (Reference pole ■Salt Bridge (5) Glass electrolytic cell Ω Electrolyte ■ KO1 saturated solution Sender: Mitsubishi Chemical Industries, Ltd. Representative Patent Attorney Hase - (7 others) Figure 1 Snake 2 Electrical route V (vs. Ay/AgC1)
Claims (1)
らなることを特徴とする固定化酵素薄膜An immobilized enzyme thin film comprising an aniline polymer having glucose oxidase.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP61070362A JPH0661266B2 (en) | 1986-03-28 | 1986-03-28 | Immobilized enzyme thin film |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP61070362A JPH0661266B2 (en) | 1986-03-28 | 1986-03-28 | Immobilized enzyme thin film |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS62228274A true JPS62228274A (en) | 1987-10-07 |
| JPH0661266B2 JPH0661266B2 (en) | 1994-08-17 |
Family
ID=13429245
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP61070362A Expired - Lifetime JPH0661266B2 (en) | 1986-03-28 | 1986-03-28 | Immobilized enzyme thin film |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH0661266B2 (en) |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0300082A2 (en) * | 1987-07-23 | 1989-01-25 | Bridgestone Corporation | Enzyme electrode |
| US5602029A (en) * | 1994-06-27 | 1997-02-11 | Nec Corporation | Method for fabricating substrate for cell culture and method for cell arrangements |
| US5942102A (en) * | 1995-11-16 | 1999-08-24 | Usf Filtration And Separations Group Inc. | Electrochemical method |
| USRE44330E1 (en) | 1995-06-19 | 2013-07-02 | Lifescan Inc. | Electrochemical cell |
-
1986
- 1986-03-28 JP JP61070362A patent/JPH0661266B2/en not_active Expired - Lifetime
Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0300082A2 (en) * | 1987-07-23 | 1989-01-25 | Bridgestone Corporation | Enzyme electrode |
| EP0300082A3 (en) * | 1987-07-23 | 1989-09-27 | Bridgestone Corporation | Enzyme electrode |
| US5602029A (en) * | 1994-06-27 | 1997-02-11 | Nec Corporation | Method for fabricating substrate for cell culture and method for cell arrangements |
| USRE44330E1 (en) | 1995-06-19 | 2013-07-02 | Lifescan Inc. | Electrochemical cell |
| US5942102A (en) * | 1995-11-16 | 1999-08-24 | Usf Filtration And Separations Group Inc. | Electrochemical method |
| USRE42567E1 (en) | 1995-11-16 | 2011-07-26 | Lifescan, Inc. | Electrochemical cell |
| US9075004B2 (en) | 1996-06-19 | 2015-07-07 | Lifescan, Inc. | Electrochemical cell |
Also Published As
| Publication number | Publication date |
|---|---|
| JPH0661266B2 (en) | 1994-08-17 |
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