JPS63106552A - Continuous quantitative analysis of creatinine and amylase - Google Patents
Continuous quantitative analysis of creatinine and amylaseInfo
- Publication number
- JPS63106552A JPS63106552A JP61251204A JP25120486A JPS63106552A JP S63106552 A JPS63106552 A JP S63106552A JP 61251204 A JP61251204 A JP 61251204A JP 25120486 A JP25120486 A JP 25120486A JP S63106552 A JPS63106552 A JP S63106552A
- Authority
- JP
- Japan
- Prior art keywords
- creatinine
- conductivity
- electrode
- change
- amylase
- 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.)
- Pending
Links
- DDRJAANPRJIHGJ-UHFFFAOYSA-N creatinine Chemical compound CN1CC(=O)NC1=N DDRJAANPRJIHGJ-UHFFFAOYSA-N 0.000 title claims abstract description 48
- 229940109239 creatinine Drugs 0.000 title claims abstract description 24
- 239000004382 Amylase Substances 0.000 title claims abstract description 22
- 102000013142 Amylases Human genes 0.000 title claims abstract description 22
- 108010065511 Amylases Proteins 0.000 title claims abstract description 22
- 235000019418 amylase Nutrition 0.000 title claims abstract description 22
- 238000004445 quantitative analysis Methods 0.000 title claims abstract 4
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 claims abstract description 28
- 239000008103 glucose Substances 0.000 claims abstract description 16
- 239000012528 membrane Substances 0.000 claims abstract description 16
- 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 abstract description 15
- 108010015776 Glucose oxidase Proteins 0.000 claims abstract description 9
- 239000004366 Glucose oxidase Substances 0.000 claims abstract description 9
- 229940116332 glucose oxidase Drugs 0.000 claims abstract description 9
- 235000019420 glucose oxidase Nutrition 0.000 claims abstract description 9
- 239000007788 liquid Substances 0.000 claims description 14
- 108010029444 creatinine deiminase Proteins 0.000 claims description 7
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 claims description 5
- 102100022624 Glucoamylase Human genes 0.000 claims description 3
- 229940071117 starch glycolate Drugs 0.000 claims description 3
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 claims 2
- 229910021529 ammonia Inorganic materials 0.000 claims 1
- 238000010924 continuous production Methods 0.000 claims 1
- 238000006911 enzymatic reaction Methods 0.000 abstract description 9
- 238000000034 method Methods 0.000 abstract description 9
- 238000006243 chemical reaction Methods 0.000 abstract description 7
- 230000000694 effects Effects 0.000 abstract description 5
- 238000005259 measurement Methods 0.000 description 16
- BASFCYQUMIYNBI-UHFFFAOYSA-N platinum Chemical compound [Pt] BASFCYQUMIYNBI-UHFFFAOYSA-N 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 238000011088 calibration curve Methods 0.000 description 4
- -1 ammonium ions Chemical class 0.000 description 3
- 238000010586 diagram Methods 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 229940079832 sodium starch glycolate Drugs 0.000 description 3
- 229920003109 sodium starch glycolate Polymers 0.000 description 3
- 239000008109 sodium starch glycolate Substances 0.000 description 3
- 239000012085 test solution Substances 0.000 description 3
- 238000003745 diagnosis Methods 0.000 description 2
- 229910052697 platinum Inorganic materials 0.000 description 2
- 229910052709 silver Inorganic materials 0.000 description 2
- 239000004332 silver Substances 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- AEMRFAOFKBGASW-UHFFFAOYSA-M Glycolate Chemical compound OCC([O-])=O AEMRFAOFKBGASW-UHFFFAOYSA-M 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- XUIMIQQOPSSXEZ-UHFFFAOYSA-N Silicon Chemical compound [Si] XUIMIQQOPSSXEZ-UHFFFAOYSA-N 0.000 description 1
- 239000013060 biological fluid Substances 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 229920002301 cellulose acetate Polymers 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 230000007661 gastrointestinal function Effects 0.000 description 1
- 235000012054 meals Nutrition 0.000 description 1
- 238000000691 measurement method Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 230000004203 pancreatic function Effects 0.000 description 1
- 239000004417 polycarbonate Substances 0.000 description 1
- 229920000515 polycarbonate Polymers 0.000 description 1
- 229920000915 polyvinyl chloride Polymers 0.000 description 1
- 239000004800 polyvinyl chloride Substances 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 229910052710 silicon Inorganic materials 0.000 description 1
- 239000010703 silicon Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910001220 stainless steel Inorganic materials 0.000 description 1
- 239000010935 stainless steel Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
Abstract
Description
【発明の詳細な説明】 〔発明の属する技術分野〕 この発明は酵素クレアチニンデイミナーゼ（Ｅ。[Detailed description of the invention] [Technical field to which the invention pertains] This invention is based on the enzyme creatinine deiminase (E.
Ｃ，３，５，１，５）を用いて被検液中のクレアチニン
を電導度法により゛定食し、リジウムスターチグリコレ
ートと酵素グルコアミラーゼ（Ｅ、Ｃ，３，２，１，：
う）と酵素電極すなわち固定化グルコースオキシダーゼ
膜−過酸化水素電極を用いてアミラーゼを定量する方法
に関する。Creatinine in the test solution was determined by the conductivity method using lysium starch glycolate and the enzyme glucoamylase (E, C, 3, 2, 1,:
c) and a method for quantifying amylase using an enzyme electrode, that is, an immobilized glucose oxidase membrane-hydrogen peroxide electrode.
この種の測定法に関連して、本件出願人は先に特開昭６
０−１５１５６０および特開昭５９−７２０５６により
クレアチニンの定食法とアミラーゼの定量法をそれぞれ
別個に提案している。前者は、試料に対してクレアチニ
ンデイミナーゼを添加することによりクレアチニンを分
解し、生成するアンモニウムイオンによる導を率の変化
量あるいは変化率を多孔性膜を有する電導度測定電極に
より検出して試料中のクレアチニンを定量するものであ
る。後者は、アミラーゼの基質としてリジウムスターチ
グリコレートと酵素グルコアミラーゼを用い、アミラー
ゼの作用により生成するグルコースを固定化グルコース
オキシダーゼ膜−過酸化水素電極により電流値の変化量
あるいは変化率として検出し、試料中のアミラーゼを定
量するものである。両者は、いずれも被検液中の共存物
質の影響を受けずにクレアチニンあるいはアミラーゼを
定量することができ、また長期間にわたり安定した測定
が行なえるといった長所がある。In connection with this type of measurement method, the present applicant has previously published
No. 0-151560 and JP-A No. 59-72056 separately propose a set meal method for creatinine and a method for quantifying amylase. In the former method, creatinine is decomposed by adding creatinine deiminase to the sample, and the amount or rate of change in conductivity due to the generated ammonium ions is detected using a conductivity measuring electrode with a porous membrane. creatinine. The latter uses lysium starch glycolate and the enzyme glucoamylase as a substrate for amylase, and detects the glucose produced by the action of amylase as the amount or rate of change in current value using an immobilized glucose oxidase membrane-hydrogen peroxide electrode. This is to quantify amylase in the sample. Both methods have the advantage of being able to quantify creatinine or amylase without being affected by coexisting substances in the test solution, and of being able to perform stable measurements over a long period of time.
しかしながら、近年臨床検を分野にたいて、生体液中の
クレアチニンとアミラーゼの測定はより正確な診断・治
療を行う上で重要視されており、両者のより簡便で迅速
・正確な定量方法が要望されている。However, in recent years, in the field of clinical examination, the measurement of creatinine and amylase in biological fluids has become important for more accurate diagnosis and treatment, and there is a need for a simpler, faster, and more accurate method for quantifying both. has been done.
本発明は上記に鑑みなされたものであり、２つの６１１
１定セル堅内において酵素反応を連続的に進め、酵素反
応による導１℃尤の変化量からクレアチニン濃度を・ま
たグルコースの変化量からアミラーゼを、互いに影響さ
れることなく正確に定量する方法を提供することである
。The present invention has been made in view of the above, and includes two 611
We developed a method to proceed with the enzyme reaction continuously in one fixed cell, and to accurately quantify creatinine concentration from the change in temperature by 1°C due to the enzyme reaction, and amylase from the change in glucose, without being influenced by each other. It is to provide.
この発明は、２つの測定セル室を用い、第１の測定セル
室において被検液に対してクレアチニンデイミナーゼを
添加することによる導電率の変化量を電導度測定電極に
より検出し、第２の測定セル室において、前記被検液に
対してさらにソジウムスターチグリコレートとグルコア
ミラーゼを添加することによるグルコースの変化量を固
定化グイコースオキシダーゼ膜−過酸化水素電極により
検出することにより、被検液中のクレアチニンとアミラ
ーゼを定量しようとするものである。This invention uses two measurement cell chambers, detects the amount of change in conductivity due to the addition of creatinine deiminase to a test liquid in the first measurement cell chamber, and detects the amount of change in conductivity by a conductivity measurement electrode. In the measurement cell chamber, the amount of change in glucose due to the addition of sodium starch glycolate and glucoamylase to the test solution is detected using an immobilized glucose oxidase membrane-hydrogen peroxide electrode. The purpose is to quantify creatinine and amylase in liquid.
第１図は本発明の一実施例である分析装置の系統図であ
る。第１図において、電導度測定セル５に電導度測定電
極１が取り付けられ、１の下端には多孔性膜３が装着さ
れている。注入ロアより被検液とクレアチニンデイミナ
ーゼ溶液を一定量注入すると次の反応が進行する。FIG. 1 is a system diagram of an analyzer that is an embodiment of the present invention. In FIG. 1, a conductivity measuring electrode 1 is attached to a conductivity measuring cell 5, and a porous membrane 3 is attached to the lower end of the conductivity measuring electrode 1. When a fixed amount of the test liquid and creatinine deiminase solution are injected from the injection lower, the next reaction proceeds.
イア ＋ Ｎ Ｈ４＋ ＯＨ−・・・・・・・・・・・
・・・・・・・・・・・・・・・・・・・・・・・・・
四・・（１）従って、被検液とクレアチニンデイミナー
ゼ溶液を注入した後送液ポンプ１３を作動させて被検液
とクレアチニンデイミナーゼ溶液を電導度測定セル５に
導き、（１）の反応により生成するアンモニウムイオン
による導電率の変化量あるいは変化率を検出しクレアチ
ニンを測定する。Ia + N H4+ OH-・・・・・・・・・・・・
・・・・・・・・・・・・・・・・・・・・・・・・
(1) Therefore, after injecting the test liquid and creatinine deiminase solution, the liquid pump 13 is activated to guide the test liquid and creatinine deiminase solution to the conductivity measurement cell 5, and the reaction of (1) is carried out. Creatinine is measured by detecting the amount or rate of change in conductivity due to ammonium ions generated.
クレアチニン測定後、送液ポンプ１３を再び作動させ、
被検液をグルコース測定セル６に導く。６にＡ酸化水素
電極２が取り付けられ、２の下端にハ固定化グルコース
オキシダーゼ膜４が装着されている。被検液中にグルコ
ースが含まれる場合には次の反応により、まず被検液中
に含まれるグルコースを電流値として測定する。After measuring creatinine, the liquid pump 13 is operated again,
The test liquid is led to the glucose measurement cell 6. A hydrogen oxide electrode 2 is attached to 6, and a fixed glucose oxidase membrane 4 is attached to the lower end of 2. When the test liquid contains glucose, the glucose contained in the test liquid is first measured as a current value by the following reaction.
被検液をグルコース測定セルに導いた後、一定時間後注
入口８よりソジウムスターヂグリコレートとグルコアミ
ラーゼ溶液を一定量注入すると次の酵素反応が進行する
。After introducing the test liquid into the glucose measurement cell, a certain amount of sodium stardi glycolate and glucoamylase solution is injected from the injection port 8 after a certain period of time, and the next enzymatic reaction proceeds.
ソジウムスターチグリコレート＋ｎ Ｈ２０ゲルコアξ
ラーゼ
ーーー−−−−→ −一一一一一−→ｎ−グルコース
・・・・・・・・・（３）従って、（３）の反応により
生成するグルコースを（２）の反応により固定化グルコ
ースオキシダーゼ膜−過酸化水素電極を用いて、電流値
の変化量あるいは変化率を検出しアミラーゼを測定する
。すなわち、電導度測定セルにおいて電導度測定電極を
用いて酵素反応による導電率の変化量あるいは変化率を
電導度測定器９により測定し、グルコース測定セルにお
いて、固定化グルコースオキシダーゼ膜−過酸化水素電
極を用いて酵素反応によるグルコースの変化量あるいは
変化率を過酸化水素測定器１０により測定し、演算器１
１で所定の演算を行うことによりクレアチニン濃度とア
ミラーゼ活性を表示器１２に表示する。Sodium starch glycolate +n H20 gel core ξ
rase---→ -11111-→n-glucose
(3) Therefore, the glucose produced by the reaction (3) can be measured by the amount of change in current value or by using the immobilized glucose oxidase membrane-hydrogen peroxide electrode by the reaction (2). Detect rate of change and measure amylase. That is, in the conductivity measuring cell, the amount or rate of change in conductivity due to the enzyme reaction is measured using the conductivity measuring electrode, and in the glucose measuring cell, the immobilized glucose oxidase membrane-hydrogen peroxide electrode is measured. The amount or rate of change in glucose due to the enzymatic reaction is measured using the hydrogen peroxide measuring device 10, and the arithmetic unit 1
By performing a predetermined calculation in step 1, the creatinine concentration and amylase activity are displayed on the display 12.
この発明に用いる電導度測定電極は、白金以外に白金−
白金黒ステンレスなどで電極間には交流電圧（好ましく
は０．５ｋＨ２，ｌ Ｖ程度）を印加して使用し、また
多孔性膜としてはポリカーボネート膜、セルロースアセ
テート膜、ボ１１ビニルクロライド膜などを用いること
ができ、好ましくは孔径０．０１５〜０．１ 、ａｍ、
膜厚２〜１０μｍである。一方、過酸化水素電極とし
ては、陽極として白金、陰極ととして銀あるいは成句化
銀が好ましく、両標間には０．６〜０．７５Ｖの一定電
圧を印加して使用し、固定化グルコースオキシダーゼ膜
としては、前記多孔性膜にグルコースを物理的あるいは
化学的に固定化したものを用いることができる。また測
定セル室は、図示されていない温度調整手段により加〜
４０°Ｃの一定温度に保たれ、さらにエアーポンプなど
によりシリコンダイヤフラムを介して攪拌されている。In addition to platinum, the conductivity measuring electrode used in this invention also includes platinum-
An alternating current voltage (preferably about 0.5 kHz, 1 V) is applied between the electrodes using platinum black stainless steel, etc., and a polycarbonate membrane, cellulose acetate membrane, polyvinyl chloride membrane, etc. is used as the porous membrane. and preferably a pore size of 0.015 to 0.1 am,
The film thickness is 2 to 10 μm. On the other hand, as the hydrogen peroxide electrode, it is preferable to use platinum as the anode and silver or silver as the cathode. As the membrane, a porous membrane with glucose physically or chemically immobilized can be used. The measurement cell chamber is also heated by a temperature control means (not shown).
The temperature is maintained at a constant temperature of 40°C, and the mixture is stirred via a silicon diaphragm using an air pump or the like.
第２図と第３図は第１図の測定系を用いた場合のクレア
チニンとアミラーゼの検量線図である。FIGS. 2 and 3 are calibration curves of creatinine and amylase when the measurement system shown in FIG. 1 is used.
第２図は電導度測定開始後４分間における導電率の変化
量とクレアチニン濃度との関係を示し、第３図はソジウ
ムスターチグリコレートトクルコアミラーゼ溶液注入後
加〜匍秒間の過酸化水素電極による電流値の変化量とア
ミラーゼ活性との関係を示す。共に良好な直線関係を示
すことから、あらかじめクレアチニンとアミラーゼそれ
ぞれについて検量線を作成しておけば未知濃度のクレア
チニンとアミラーゼを簡単に定量することができる。Figure 2 shows the relationship between the amount of change in conductivity and creatinine concentration for 4 minutes after the start of conductivity measurement, and Figure 3 shows the relationship between the hydrogen peroxide electrode and the creatinine concentration after injection of the sodium starch glycolate tocurcoamylase solution. The relationship between the amount of change in current value and amylase activity is shown. Since both show a good linear relationship, if a calibration curve is created for each of creatinine and amylase in advance, unknown concentrations of creatinine and amylase can be easily quantified.
なお、前記実施例においては、導電率の変化量を検出す
る工程を先に行っているが、本発明はこれに限られるも
のではなく、先に酵素反応によるグルコースの変化ｔｉ
検出する工程を行った後、導電率の変化量を検出する工
程を行うことも可能である。In the above embodiments, the step of detecting the amount of change in electrical conductivity is performed first, but the present invention is not limited to this.
After performing the step of detecting, it is also possible to perform the step of detecting the amount of change in conductivity.
以上の説明から明らかなようにこの発明によれば、２つ
の測定セルを用い被検液に対して異なる酵素反応を連続
的に進行させ、それぞれの反応による導ｉ１１藁および
過酸化水素の変化量あるいは変化率を検出し、クレアチ
ニンとアミラーゼを定量することとしたため、簡単な操
作でじん蔵およびすい蔵機能の診断に欠かすことのでき
ないクレアチニンとアミラーゼを、少量の被検液で互い
に影響されることなく簡便で迅速・正確に定量すること
ができる。また被検液として血液と尿を測定することが
でき、この場合にはアミラーゼとクレアチニンのクリア
ランス比を容易に求めることができ、より正確な診断・
治療に寄与するという効果が得られる。As is clear from the above description, according to the present invention, two measurement cells are used to continuously carry out different enzyme reactions on the test liquid, and the amount of change in the concentration of hydrogen peroxide and hydrogen peroxide due to each reaction is Alternatively, by detecting the rate of change and quantifying creatinine and amylase, it is possible to easily measure creatinine and amylase, which are essential for diagnosing gastrointestinal and pancreatic functions, by detecting their mutual influence in a small amount of test liquid. It can be easily, quickly, and accurately quantified. In addition, blood and urine can be measured as test fluids, and in this case, the clearance ratio between amylase and creatinine can be easily determined, allowing for more accurate diagnosis and
The effect of contributing to treatment can be obtained.
第１図は本発明の一実施例を示す分析装置の系統図、第
２図は第１図の分析装置によるクレアチニンの検量線図
、第３図は第１図の分析装置によるアミラーゼの検量線
図である。
１・・・電導度測定電極、２・・・過酸化水素測定電極
、３・・・多孔性膜、４・・・固定化グルコースオキシ
ダーゼ膜、５・・・電導度測定セル、６・・・グルコー
ス測定セル、９・・・電導度測定器、１０・・・過酸化
水素測定器、１】・・・演算器、１２・・・表示器。
第１０Fig. 1 is a system diagram of an analyzer showing an embodiment of the present invention, Fig. 2 is a calibration curve for creatinine using the analyzer shown in Fig. 1, and Fig. 3 is a calibration curve for amylase using the analyzer shown in Fig. 1. It is a diagram. DESCRIPTION OF SYMBOLS 1... Conductivity measurement electrode, 2... Hydrogen peroxide measurement electrode, 3... Porous membrane, 4... Immobilized glucose oxidase membrane, 5... Conductivity measurement cell, 6... Glucose measuring cell, 9... Conductivity measuring device, 10... Hydrogen peroxide measuring device, 1]... Arithmetic unit, 12... Display device. 10th
Claims (1)
とによりクレアチニンを分解し、生成するアンモニアに
よる導電率の変化量を多孔性膜を有する電導度測定電極
により検出する工程と、前記被検液に対してリジウムス
ターチグリコレートとグルコアミラーゼを添加反応させ
、生成するグルコースの変化量を固定化グルコースオキ
シダーゼ膜−過酸化水素電極により検出する工程とを連
続して行うことを特徴とするクレアチニンとアミラーゼ
の連続定量法。A step of decomposing creatinine by adding creatinine deiminase to the test liquid and detecting the amount of change in conductivity due to the generated ammonia using a conductivity measuring electrode having a porous membrane; A continuous process of creatinine and amylase, characterized in that the steps of adding and reacting lysium starch glycolate and glucoamylase and detecting the amount of change in the produced glucose using an immobilized glucose oxidase membrane and a hydrogen peroxide electrode are performed continuously. Quantitative method.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP61251204A JPS63106552A (en) | 1986-10-22 | 1986-10-22 | Continuous quantitative analysis of creatinine and amylase |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP61251204A JPS63106552A (en) | 1986-10-22 | 1986-10-22 | Continuous quantitative analysis of creatinine and amylase |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPS63106552A true JPS63106552A (en) | 1988-05-11 |
Family
ID=17219240
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP61251204A Pending JPS63106552A (en) | 1986-10-22 | 1986-10-22 | Continuous quantitative analysis of creatinine and amylase |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS63106552A (en) |
-
1986
- 1986-10-22 JP JP61251204A patent/JPS63106552A/en active Pending
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