JPS59228158A - Neutral lipid sensor - Google Patents

Neutral lipid sensor

Info

Publication number
JPS59228158A
JPS59228158A JP58103248A JP10324883A JPS59228158A JP S59228158 A JPS59228158 A JP S59228158A JP 58103248 A JP58103248 A JP 58103248A JP 10324883 A JP10324883 A JP 10324883A JP S59228158 A JPS59228158 A JP S59228158A
Authority
JP
Japan
Prior art keywords
neutral lipid
solution
sensor
immobilized enzyme
blood serum
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
Application number
JP58103248A
Other languages
Japanese (ja)
Other versions
JPH043501B2 (en
Inventor
Masao Karube
征夫 軽部
Etsuo Ozaki
尾崎　悦夫
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Jeol Ltd
Original Assignee
Jeol Ltd
Nihon Denshi KK
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by Jeol Ltd, Nihon Denshi KK filed Critical Jeol Ltd
Priority to JP58103248A priority Critical patent/JPS59228158A/en
Publication of JPS59228158A publication Critical patent/JPS59228158A/en
Publication of JPH043501B2 publication Critical patent/JPH043501B2/ja
Granted legal-status Critical Current

Links

Classifications

    • 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

Abstract

PURPOSE:To measure the density of neutral lipid contained in blood serum etc. at a high accuracy by using lipoprotein lipase and glycerol oxidase as immobilized enzyme. CONSTITUTION:A teflon membrane 4 which transmits oxygen molecules is installed to the bottom of the outer tube 2 of a neutral lipid sensor, and outside the teflon memberane, a neutral lipid transmission membrane 7 containing immobilized engyme mixed with lipoprotein lipase and glycerol oxidase is provided. This neutral lipid sensor is immersed in a solution and blood serum specimen is injected, then neutral lipid contained in the blood serum reacts with water in the solution with lipoprotein lipase in the immobilized enzyme used as a catalyst. By this reaction, glycerose and fatty acid are produced, and glycerose reacts with oxygen in the solution with glycerol oxidase in the immobilized enzyme used as a catalyst and produces glyceryl aldehyde and hydrogen peroxide. As a result of this, a current between a cathode 3 and an anode 2 decreases and neutral lipid can be measured.

Description

【発明の詳細な説明】 本発明は、簡単に血清等に含まれる中性脂質の濃度を測
定Ｊることができる固定化酵素を利用した中性脂質セン
サーに関り′る。DETAILED DESCRIPTION OF THE INVENTION The present invention relates to a neutral lipid sensor using an immobilized enzyme that can easily measure the concentration of neutral lipids contained in serum or the like.

従来、固定化酵素を利用した中性脂質分析には、固定化
酵素カラムとｐＨ電極を組合Ｕたシス′）ム。Conventionally, neutral lipid analysis using immobilized enzymes uses a system that combines an immobilized enzyme column and a pH electrode.

固定化酊累膜ど酸素電極あるい１ｊ過酸化水止（１１２
０２）電極とを組合せたシステムとが利用されている。Immobilized oxygen electrode or 1j peroxide water stopper (112
02) A system combining electrodes is used.

前者のシステムは、１）１１電極を使用し−（おり、測
定がボテンショメ１〜リンクであるｌこめに測定粕１哀
が充分でなく、又、カラムを用いろＩこめ、ポンプや検
出のためのフローレルが必ザとイｊす、システ１１が大
型どなる。一方後省のシス７１＼は、被測定溶媒中に溶
１）込んでいるＦ１１２素分子、あるいは過酸化水素を
電解し、その肋の電解電流を測定りるようにしくおり、
アンベＵメｌヘリツクな測定（・あるために高い精度で
測定を行うことがぐさイ５０しかしながら、中性脂質か
ら過酸化水素を牛成りるまでの反応系が複雑であり、測
定の途中で多数の試薬を溶液中に添加しな（プればなら
ず、複雑り作業が要求される。The former system 1) uses 11 electrodes, and there is not enough lees to be measured when the measurement is at the bottom of the link, and also a column is used for pumping and detection. The system 11 makes a loud roar when the Florel of Florel is forced to do so.Meanwhile, the later system 71\ electrolyzes the F112 elementary molecules or hydrogen peroxide dissolved in the solvent to be measured, and It is designed to measure the electrolytic current of
However, the reaction system from neutral lipids to hydrogen peroxide is complex, and many reagents must be added to the solution, which requires complicated operations.

本発明は、上述した点に鑑みでなされ！、：も−ので、
簡単に高い精瓜で中性脂質を測定づることがでさる中性
脂質はンザーを提供することを目的とＪる。The present invention has been made in view of the above points! , :Mo-so,
The purpose of this study is to provide a neutral lipid sample that can be easily measured in high-quality melon.

本発明看は、中性脂質がリボプロティンリパーゼ（Ｌ　
１ｐｏｐｒｏｒｅｉｎ　　１ｉｐａｓｅ）を触媒として
水（１」２０）と反応し、グリセロール（Ｇ　１ｙｃｅ
ｒｏｌ　）と脂肪酸が生成されること、該生成されたグ
リセロールがグリセ１」−ルＡ４．シダー１２　（Ｑ　
１ｙｃｅｒｏｌｏｘｉｄａｓｅ　）を触媒として酸素分
子（０２）と反応し、グリヒルアルデハイド（Ｑ　１ｙ
ｃｅｒａｌｄｅ１１ｙｄｅ　）と過酸化水素（１１＋　
０２　）を生成すること、及びこの２番目の反応による
溶液中の酸素量の減少あるいは、過酸化水素量の増加を
検出づ−ることにより、該中性脂質のｍ、　（ｌｃ＝　
ＩＯ）を簡単に測定することができることを見出した。In the present invention, the neutral lipid is riboprotein lipase (L
1poprorein 1ipase) is used as a catalyst to react with water (1'20), and glycerol (G 1yce
rol) and fatty acids are produced, and the produced glycerol is glycerol A4. Cedar 12 (Q
1yceroloxidase) as a catalyst and reacts with oxygen molecules (02) to form glycyraldehyde (Q1y
ceralde11yde) and hydrogen peroxide (11+
m, (lc=
It has been found that IO) can be easily measured.

従って、本発明に基づく中性脂質センサーは、第１と第
２の電極を有し、その一方の電極近傍に固定化酵素を配
置し、該電極間に流れる電流に以づい−Ｃ１被測定溶液
中に含まれる中性脂質を測定づるようにしたセンサーに
（Ｉ３いて、該固定化酵素として、リボプロディンリパ
ーゼとグリセロールオキシダーＵを用いたことを特徴と
している。Therefore, the neutral lipid sensor based on the present invention has first and second electrodes, an immobilized enzyme is placed near one of the electrodes, and the current flowing between the electrodes causes -C1 to be measured in the -C1 solution. The sensor (I3) is designed to measure the neutral lipids contained therein, and is characterized by the use of riboprodin lipase and glycerol oxider U as the immobilized enzymes.

以上本発明の一実施例を添（＝１図面に工１１づさ計速
づる。The above is an example of the present invention.

第１図（よ、本発明に基づ゛く中＋’ｌ脂ｙＴレンセン
どしての酸素電極を示しており、′１はガラス製の内管
、２は同じくガラス製の外管であり、該内管′１の底部
には、白金製のカソード（第１電極）　１３が設けられ
、又、該外管２の底部には、酸木分イを透過り一ζテフ
ロン１．膜４が取イ」（プられＣいる。該内管１と該外
管２との間に１よ、内部液（：（（１％Ｎａ（’）１−
１）５が入れられ、該内部液中には、鉛製の７７ノード
（第２電極）６が配にＩさね（いる。該カソード３．ア
ノード６には夫々白金のリード線１０が取イ」りられ（
いる。該酸素の了透過↑４の−ｊ〕１１ン膜の外側には
、中性脂質が透過′Ｃ−さる透析ＩＩＩ！　７　ｊ〕一
般）フられ、その中にはりボブ［」ｊインリパーゼとグ
リセロールオキシダーゼとが渥含された固定化酵素８が
入れられている。尚、９１．、Ｌ　ＯリングＫ・ｒ１９
る。Fig. 1 shows an oxygen electrode such as a medium-high temperature sensor according to the present invention, where 1 is an inner tube made of glass, and 2 is an outer tube also made of glass. A cathode (first electrode) 13 made of platinum is provided at the bottom of the inner tube '1, and a 1ζ Teflon membrane 4 is provided at the bottom of the outer tube 2. There is an internal liquid (:((1%Na(')1-) between the inner tube 1 and the outer tube 2.
1) 5 is placed, and 77 lead-made nodes (second electrodes) 6 are placed in the internal liquid. Platinum lead wires 10 are attached to the cathodes 3 and anodes 6, respectively. i” Rirare(
There is. Neutral lipids are permeated on the outside of the membrane through which oxygen permeates ↑4-j]11 Dialysis III! 7j] General) An immobilized enzyme 8 containing both inlipase and glycerol oxidase is placed therein. Furthermore, 91. , L O-ring K・r19
Ru.

第２図は、上述したセンサーどしでの酸素電極１１を用
いた中性脂質測定システ１１の一例を示している。該酸
素電極１１は、３０’Ｃに維持された水ＩＱ１２中に配
置されでいるビー力１３内に挿入される。該じ一力１３
内の溶液中には、テフロンがコーフーイング凸れたＩａ
性鉢体１７１入れられており、該ビー力１３の下部に設
りられだ回転磁場発生装置１５にＪ、る回転！１揚にＪ
、す、該磁性体１４は回転し、その結果、該ビー力１３
中の溶液は攪拌される。該酸素電極１１の第１と第２の
電極間に流れた電θ＋ｊＩＪ、△−Ｖ変換器１６によっ
て電圧信号に変換され、レニ１−ダ１７に供給される。FIG. 2 shows an example of the neutral lipid measurement system 11 using the oxygen electrodes 11 with the above-mentioned sensors. The oxygen electrode 11 is inserted into a bea force 13 which is placed in water IQ 12 maintained at 30'C. Same power 13
In the solution inside, Teflon has a convex convex Ia.
The magnetic pot body 171 is inserted into the rotary magnetic field generator 15 installed at the bottom of the bead 13 and rotates! J for 1 frying
, the magnetic body 14 rotates, and as a result, the beam force 13
The solution inside is stirred. The electric current θ+jIJ flowing between the first and second electrodes of the oxygen electrode 11 is converted into a voltage signal by the Δ-V converter 16 and supplied to the encoder 17.

尚、１８は測定試７３＋をビーカゴ３内に注入りるため
のマイクロシリンジ（・ある。Note that 18 is a microsyringe for injecting the measurement sample 73+ into the beaker 3.

上述した如さ」１１１成において、ビーカゴ３内に酸素
電極１１を挿入し、磁性体１４を回転させＣ該ビーカ内
の溶液の攪拌を行う。該１ｔ１２拌により、該ビーカ１
３内部の溶液中の酸系濃度はプラトーの状態となり、ぞ
の後、マイクロシリンジ１８より血清が該溶液中にンー
１人される。該血泊中に含まれる中性脂質は、該酸素電
極１１底部に設（プられている固定化酵素の内のりボブ
１］テインリパーピを触媒として識溶液中の水と反応り
る。この反応により、グリセ［」−ルと脂肪酸がイ１成
、＼１′シるが、１−１曳生成されたグリセロールは、
固定化耐糸の内のグリセロールオキシダーゼを触媒とし
く該溶液中の酸比分子と反応し、グリセルアル）゛ハイ
ドど逮）酸化水素を生成づる。この結果、酸）：６０ｆ
、底）１１；のカソード３周辺の酸素分子の量（淵麿）
は、該２番目の反応によって少くなり、該カソード３と
アノード１どの間に流れる電流は低く　’＜４−る。数
分の後、該電流値はプラトーの状態と（＜す、グリセロ
ールとの反応に？ｊ与りる酵素の吊に比例し）こ該？ｔ
ｉ流碩の変化から、中性脂質のＭ（濃ｊ良）を測定リイ
２ことができる１゜ 次に実験例を示づ。As described above, in step 111, the oxygen electrode 11 is inserted into the beaker 3, and the magnetic body 14 is rotated to stir the solution in the beaker. By the 1t12 stirring, the beaker 1
The acid concentration in the solution inside 3 reaches a plateau state, and after that, serum is poured into the solution from the microsyringe 18. The neutral lipids contained in the blood react with water in the blood solution using the immobilized enzyme disposed at the bottom of the oxygen electrode 11 as a catalyst. [''-ru and fatty acids are formed in 1,\1', but the glycerol produced in 1-1 is,
Glycerol oxidase in the immobilized yarn reacts with acidic molecules in the solution as a catalyst to generate glyceral, hydride, etc. hydrogen oxide. As a result, acid): 60f
, bottom) 11; amount of oxygen molecules around cathode 3 (Fuchimaro)
is reduced by the second reaction, and the current flowing between the cathode 3 and the anode 1 is low. After a few minutes, the current value reaches a plateau (proportional to the rate of the enzyme participating in the reaction with glycerol). t
The M (concentration) of neutral lipids can be measured from the change in flow.Next, an experimental example is shown.

実施例 人コントロール面清のイ釈系列を試別としく、本発明に
基づくセンサーの特性を調べた。＝１ン（〜ロール血清
は、栄研化学（株）製すビッドト−゛ツムｌを用いた。EXAMPLE The characteristics of the sensor based on the present invention were investigated using a series of infusions from human control surfaces as a trial. = 1 ton (~Roll) As the serum, Vidtorm l manufactured by Eiken Kagaku Co., Ltd. was used.

分析条件は、Ｗ衝液：Ｑ、ＩＭ。The analysis conditions were W buffer: Q, IM.

１）Ｎ８．Ｑリン酸緩衝液（トリｌ−ンＸ１００４％）
、反応温Ｕ：３０℃、試イ′＋１♀：５０μ妃であった
。1) N8. Q phosphate buffer (Trine X 1004%)
, reaction temperature U: 30°C, trial temperature: 50μ.

各濃度にＪ５１ノる応答曲線を第３図に示づが、この図
におい゛（、縦Ｑ＋１＋は検出電流値（μ△）、横軸は
［１（分）である。第１Ｉ図（３Ｌ、第３図の測定結果
に基づいて得られた電流価差ど濃度との関係を示リグラ
フであり、このグラフを用い、未知試料中の中１ｉ脂質
の濃度を求めることかできる。尚、この試験の同時再現
性は、５回の測定℃゛相対標準偏差饋６．６％であった
。The response curve of J51 to each concentration is shown in Figure 3. , is a graph showing the relationship between the current value difference and the concentration obtained based on the measurement results in Figure 3. Using this graph, the concentration of medium 1i lipid in an unknown sample can be determined. The reproducibility of the test was 6.6% relative standard deviation °C for 5 measurements.

（試験例２） イ匁４（的中す１１脂７’、ｉ　Ｉ／）　１つて′ある
１〜リオレインを試料とじ（本発明に基づくセンリーー
の特性を調べｌこ。(Test Example 2) I momme 4 (hit 11 fat 7', i I/) One sample bound 1 to lyolein (investigate the characteristics of Senley based on the present invention).

トリスレインは東京化成（株）製のものを使用した。分
析条イ′１（緩町液９反応温磨、試判量）は、上述した
試験例１ど同じでｄうり、この試験の結果得られた検量
線を第５ｑに示づ。尚、この時の同時再現性は、５回の
測定で相対標準偏差（１ｆ５．７％であった。Trislane manufactured by Tokyo Kasei Co., Ltd. was used. Analysis strip A'1 (Yurumachi solution 9 reaction temperature, test amount) was the same as in Test Example 1 described above, and the calibration curve obtained as a result of this test is shown in No. 5Q. Incidentally, the simultaneous reproducibility at this time was a relative standard deviation (1f5.7%) in 5 measurements.

（試験例３） 試料としての人血れ！■を本発明に基づくセンサ゛−と
従来法によって分析し、比較した１２分析条ｉ′１（緩
衝液１反応温庶、試１１年）は°、１−記試験例１ど同
じて・あり、検量線は、試験例ＩＣｌ：？られたしのを
使用した。この分析結果を人’ｌ　ｌｊ−、；＋、・Ｊ
か、Ｊ゛５、のｄｉ　１ｉン（、上、ｍｑ／ｄｌ−（”
ある。尚、従来法と（，１、自動化学分析装置を用い、
試お１ど酵バ・、試桑どを′置台しく反応８υ−１反応
溶液をＩｆ：　ｅ　ａｉ１１定したしの（：ある。(Test Example 3) Human blood as a sample! (1) was analyzed using the sensor based on the present invention and the conventional method, and the 12 analytical samples i'1 (buffer solution 1 reaction temperature, 11 years of testing) were the same as in Test Example 1. The calibration curve is test example ICl:? I used the one that was made. The results of this analysis can be expressed as follows:
Or, J゛5, di 1in (, top, mq/dl-(”
be. In addition, the conventional method and (1) using an automatic chemical analyzer,
Place the first fermentation vessel and the first sample on the stand, and the reaction solution 8υ-1 is determined as If: e ai11.

以上詳述した如く、本発明ｆｊ：　、Ｊ、、　ＩＩば、
固）」−°化醇素どしてリポプロディンリバーじどグリ
し・［１−ルＡキシダー口を用いる簡ｊｌ’ｉな１☆１
成で、１ｉ＋ｉ：ｌ脂τ：１の検出をアンベロメ］−リ
ックに１６〒１゛白％（行うことｉ＋・でさる。尚、本
発明は上述した実施例に限定、＼４′；ることなく幾多
の変形が可能（・ある。例えば、ハ！：索電掩を使用せ
ず、グリヒＬ〕−ルと酸素との反応によっ−（生成され
る過酸化水素を検出覆るための過酸化水素電極を用いて
も良い。又、測定システムは第２図の４ｙ４成に限定さ
れないもので、溶液の撹拌手段、試料の注入手段６９は
、他の機構を用いることができる。As detailed above, the present invention fj: , J, II,
1-1-Simple 1☆1 using oxidizer mouth
The detection of 1i+i:l fat τ:1 is carried out at 16〒1゛white% (by i+・.The present invention is limited to the above-mentioned embodiment; (There are many variations possible. For example, Ha!: By the reaction of glycol and oxygen without using an electric cable (peroxide to detect and cover the generated hydrogen peroxide) A hydrogen electrode may be used.Also, the measurement system is not limited to the 4y4 configuration shown in FIG. 2, and other mechanisms may be used as the solution stirring means and sample injection means 69.

【図面の簡単な説明】[Brief explanation of drawings]

第１図は、本発明に赫づくセンサーの一実施例を示１図
、第２図は中性脂質測定システムの一例１・・・内ｉ”
”、２・・・外管 ３３・・・カソード ４・・・酸素ガス透過性膜 ６・・・）ノノード　　　７・・・透析膜８・・・固定
化酵素 １１・・・ｈシ桑電極　　１２・・・水槽１３・・・ビ
ー力　　　１４・・・磁性体１５・・・回転磁場発生装
置 １６・・・八−Ｖ変換器 １７・・・し］−ダ １８・・・ンイクロシリンジ 特許出願人 日本電子株式会７１ 代表者　１’Ｊ’　ＩＩ！　　−人 石 第２図 ｕ　　　　　＋ｏｏ　　　　ｚｏｏ　　　Ｊｌ）Ｃ１４
ｏｏ　　　　ｓｏ。 第５１ （ＪＡ） ５０　　　　２（ （ｍ。 閃 一〇 ２／、、ｔｔ）Fig. 1 shows an example of a sensor according to the present invention, and Fig. 2 shows an example of a neutral lipid measuring system.
", 2... Outer tube 33... Cathode 4... Oxygen gas permeable membrane 6...) Nonode 7... Dialysis membrane 8... Immobilized enzyme 11... h Mulberry electrode 12 ... Water tank 13 ... Bee force 14 ... Magnetic body 15 ... Rotating magnetic field generator 16 ... Person Japan Electronics Co., Ltd. 71 Representative 1'J' II! -Jinseki 2nd figure u +oo zooo Jl)C14
oo so. 51st (JA) 50 2 ((m. Sen 102/,, tt)

Claims (3)

【特許請求の範囲】[Claims] （１）第１と第２の電極を有し、その一方の電極近傍に
固定化酵素を配回し、該電極間に流れる電流に基づいて
、被測定溶液中に含まれる中性脂質を測定するようにし
たセンサーにおいて、該固定化酵素として、リボプロテ
ィンリパーゼとグリセロールＡキシダーピを用い！ここ
とを特徴と覆る中性脂質センサー。(1) It has a first and second electrode, an immobilized enzyme is placed near one of the electrodes, and the neutral lipid contained in the solution to be measured is measured based on the current flowing between the electrodes. In this sensor, riboprotein lipase and glycerol A oxidase are used as the immobilized enzymes! A neutral lipid sensor that covers this feature. （２）該両電極間に流れる電流は、該一方の電極近傍の
酸素の量に応じて変化づる特許請求の範囲第１項記載の
中性脂質センナ−０(2) The current flowing between the two electrodes changes depending on the amount of oxygen near the one electrode. （３）該両電極間に流れる電流は、該一方の電極近傍の
過酸化水素の辺に応じて変化する特許請求の範囲第１項
記載の中性脂質センサー。(3) The neutral lipid sensor according to claim 1, wherein the current flowing between the two electrodes changes depending on the side of hydrogen peroxide near the one electrode.
JP58103248A 1983-06-09 1983-06-09 Neutral lipid sensor Granted JPS59228158A (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
JP58103248A JPS59228158A (en) 1983-06-09 1983-06-09 Neutral lipid sensor

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP58103248A JPS59228158A (en) 1983-06-09 1983-06-09 Neutral lipid sensor

Publications (2)

Publication Number Publication Date
JPS59228158A true JPS59228158A (en) 1984-12-21
JPH043501B2 JPH043501B2 (en) 1992-01-23

Family

ID=14349137

Family Applications (1)

Application Number Title Priority Date Filing Date
JP58103248A Granted JPS59228158A (en) 1983-06-09 1983-06-09 Neutral lipid sensor

Country Status (1)

Country Link
JP (1) JPS59228158A (en)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US9957542B2 (en) 2005-03-29 2018-05-01 Cci Corporation Biosensor

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US9957542B2 (en) 2005-03-29 2018-05-01 Cci Corporation Biosensor

Also Published As

Publication number Publication date
JPH043501B2 (en) 1992-01-23

Similar Documents

Publication Publication Date Title
Gough et al. Membrane-covered, rotated disk electrode
US4003705A (en) Analysis apparatus and method of measuring rate of change of electrolyte pH
US4415666A (en) Enzyme electrode membrane
US4040908A (en) Polarographic analysis of cholesterol and other macromolecular substances
JP2646848B2 (en) Glucose sensor measurement method
US4065357A (en) Detection of catalase-containing bacteria
EP0020623B1 (en) Analytical process and means for measuring the amount of hydrogen peroxide in aqueous media and of organic substrates generating hydrogen peroxide by enzymatic oxidation
CA1191898A (en) Method for measuring ionic concentration utilizing an ion-sensing electrode
US3838034A (en) Apparatus for detection of catalase-containing bacteria
Satoh et al. Enzyme electrode for free cholesterol
JPH09500450A (en) Method and device for electrochemical measurement
WO1994002842A1 (en) Analytical method for the detection and measurement of paracetamol
Durliat et al. Reagentless amperometric lactate electrode
US6043878A (en) Device for optical and electrochemical measurements in microliter size samples
Pemberton et al. An assay for the enzyme N-acetyl-β-D-glucosaminidase (NAGase) based on electrochemical detection using screen-printed carbon electrodes (SPCEs)
OsAKAI et al. A novel amperometric urea sensor
JPS59228158A (en) Neutral lipid sensor
JPS5861459A (en) Analyzing device for creatine and creatinine
Jaenchen et al. An Electrochemical Determination of Uric Acid in Sera by a Flow-Through Equipment with and Without Uricase
JPH0432608Y2 (en)
JPS636457A (en) Method for testing enzyme activity of immobilized enzyme film
JPS59228157A (en) Phospholipid sensor
Delgado et al. An ultrasensitive electrometric system to measure membrane-bound acetylcholinesterase activity
JPH0418621B2 (en)
RU2249818C2 (en) Protein content determination method