JP2714143B2 - Immunological measurement method - Google Patents
Immunological measurement methodInfo
- Publication number
- JP2714143B2 JP2714143B2 JP1150743A JP15074389A JP2714143B2 JP 2714143 B2 JP2714143 B2 JP 2714143B2 JP 1150743 A JP1150743 A JP 1150743A JP 15074389 A JP15074389 A JP 15074389A JP 2714143 B2 JP2714143 B2 JP 2714143B2
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- Prior art keywords
- amylase
- antibody
- antigen
- labeled
- sample
- 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.)
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Description
【発明の詳細な説明】 〔産業上の利用分野〕 本発明は、新しいB/F分離方法を用いて抗原又は抗体
を特異的に測定するようにした免疫学的測定方法に関す
る。DETAILED DESCRIPTION OF THE INVENTION [Industrial Application Field] The present invention relates to an immunological assay method for specifically measuring an antigen or an antibody using a new B / F separation method.
抗原抗体反応を利用した免疫測定方法としてEIA法が
近年急激に行われるようになった。EIA法においては、
通常ビーズ、プレート、磁性粒子、シリコン、ガラス、
ディスク、濾紙等の不溶性担体に固定化した抗原又は抗
体を用いて検体中の微量成分、例えば、CEA、インシュ
リン、HBs抗原、HBs抗体を正確に測定できるようになっ
た。このようなビーズ等の不溶性担体を用いた測定法
は、抗原抗体反応によって結合した物質（Bound）と結
合していない物質（Free）の分離（B/F分離）の操作を
行った後に、試料中の微量成分を測定する。よく使われ
ている２ステップサンドイッチ法では、これはあらかじ
め抗原又は第一抗体を固定化した不溶性担体に試料中の
抗体又は抗原を反応させ、洗浄後、酵素標識第二抗体を
加え反応させる。この不溶性担体を十分に洗浄すること
によってB/F分離を行い、基質を加え酵素活性測定する
ことによって試料中の抗原又は抗体を測定することがで
きる。In recent years, the EIA method has been rapidly performed as an immunoassay method using an antigen-antibody reaction. In the EIA law,
Usually beads, plates, magnetic particles, silicon, glass,
By using an antigen or an antibody immobilized on an insoluble carrier such as a disc or filter paper, a trace component in a sample, for example, CEA, insulin, HBs antigen, and HBs antibody can be accurately measured. The measurement method using an insoluble carrier such as a bead is a method of separating a substance bound by an antigen-antibody reaction (Bound) and a substance not bound (Free) (B / F separation), and then performing sample separation. Measure the trace components in it. In a commonly used two-step sandwich method, an antibody or an antigen in a sample is reacted with an insoluble carrier on which an antigen or a first antibody is immobilized in advance, and after washing, an enzyme-labeled second antibody is added and reacted. The B / F separation is performed by sufficiently washing the insoluble carrier, and the antigen or antibody in the sample can be measured by adding the substrate and measuring the enzyme activity.
また、第一抗体、第二抗体ともにモノクロナール抗体
を用いれば、同時に第一抗体を固定化した不溶性担体に
検体と酵素標識第二抗体を同時に加えることができ、抗
原抗体反応を一段階で済ませることができるので、操作
時間が２ステップサンドイッチより短くて済み、手間も
省ける。If a monoclonal antibody is used for both the first antibody and the second antibody, the specimen and the enzyme-labeled second antibody can be simultaneously added to the insoluble carrier on which the first antibody is immobilized, thereby completing the antigen-antibody reaction in one step. The operation time is shorter than that of a two-step sandwich, and labor can be saved.
最近、酸化鉄等の磁性粒子を用いて磁石によってB/F
分離を迅速に行う方法がEIA自動分析装置に応用される
ようになった。Recently, B / F by magnet using magnetic particles such as iron oxide
Rapid separation methods have been applied to EIA automated analyzers.
本発明は、従来のように抗原抗体反応を固相上で行わ
せるのではなく、液相での反応を用いかつB/F分離を容
易に行うことによって、操作性、時間短縮をはかり、さ
らには自動化を容易に行う目的で発明されたものであ
る。The present invention, instead of allowing the antigen-antibody reaction to be performed on a solid phase as in the prior art, by using a reaction in a liquid phase and easily performing B / F separation, achieves operability and time reduction. Has been invented for the purpose of facilitating automation.
本発明は、吸着体、例えば澱粉のアミラーゼに対する特
異的な結合性に着目しB/F分離を容易かつ迅速に行うこ
とが可能となることを見出し完成されたものである。The present invention has been completed by finding that it is possible to easily and rapidly perform B / F separation by focusing on the specific binding of an adsorbent, for example, starch to amylase.
本発明は、抗原抗体反応時において液層での反応が可
能であることにより反応時間で短縮でき、試料中の微量
成分と抗原抗体反応によって生じたアミラーゼ標識抗体
−抗原−非アミラーゼ標識抗体の抗原抗体反応複合物を
アミラーゼを介して澱粉等の吸着体に吸着してB/F分離
を容易かつ迅速に行い、当該微量成分を極めて効率的に
測定できるようにし、また自動化を容易に行うための免
疫学的測定方法を提供することを目的とする。The present invention is capable of shortening the reaction time by allowing a reaction in a liquid layer at the time of antigen-antibody reaction, and the amylase-labeled antibody-antigen-antigen of non-amylase-labeled antibody generated by the antigen-antibody reaction with a trace component in the sample. The antibody reaction complex is adsorbed onto an adsorbent such as starch via amylase to perform B / F separation easily and quickly, so that the trace components can be measured extremely efficiently, and to facilitate automation. It is intended to provide an immunological measurement method.
上記目的を達成するため、本発明の免疫学的測定方法
の第１の態様においては、試料中の抗原に特異的な非ア
ミラーゼ標識抗体とアミラーゼ標識抗体を反応させた
後、アミラーゼに結合性の強い吸着体によりB/F分離を
行い該吸着体に吸着した非アミラーゼ標識抗体の標識活
性により試料中の抗原を測定するものである。本発明の
免疫学的測定方法の第２の態様においては、試料中の抗
体に特異的な非アミラーゼ標識抗原とアミラーゼ標識抗
原を反応させた後、アミラーゼに結合性の強い吸着体に
よりB/F分離を行い該吸着体に吸着した非アミラーゼ標
識抗原の標識活性により試料中の抗体を測定するもので
ある。本発明の免疫学的測定方法の第３の態様において
は、試料中の抗原と競合する非アミラーゼ標識抗原とア
ミラーゼ標識抗体を反応させた後、アミラーゼに結合性
の強い吸着体によりB/F分離を行い該吸着体に吸着した
非アミラーゼ標識抗原の標識活性により試料中の抗原を
測定するものである。本発明の免疫学的測定方法の第４
の態様においては、試料中の抗体と競合する非アミラー
ゼ標識抗体とアミラーゼ標識抗原を反応させた後、アミ
ラーゼに結合性の強い吸着体によりB/F分離を行い該吸
着体に吸着した非アミラーゼ標識抗体の標識活性により
試料中の抗体を測定するものである。In order to achieve the above object, in the first embodiment of the immunological assay method of the present invention, after reacting an amylase-labeled antibody with a non-amylase-labeled antibody specific for an antigen in a sample, B / F separation is performed by a strong adsorbent, and the antigen in the sample is measured by the labeling activity of the non-amylase-labeled antibody adsorbed on the adsorbent. In the second embodiment of the immunological measurement method of the present invention, after reacting a non-amylase-labeled antigen specific to an antibody in a sample with an amylase-labeled antigen, B / F The antibody in the sample is measured based on the labeling activity of the non-amylase-labeled antigen adsorbed on the adsorbent after separation. In the third embodiment of the immunological assay method of the present invention, after reacting a non-amylase-labeled antigen that competes with an antigen in a sample with an amylase-labeled antibody, B / F separation is performed using an adsorbent having strong amylase binding properties. And measuring the antigen in the sample based on the labeling activity of the non-amylase-labeled antigen adsorbed on the adsorbent. Fourth Method of the Immunological Measurement Method of the Present Invention
In the embodiment, after reacting a non-amylase-labeled antibody and an amylase-labeled antigen that compete with the antibody in the sample, the non-amylase label adsorbed on the adsorbent is subjected to B / F separation by an adsorbent having strong binding to amylase. The antibody in the sample is measured by the labeling activity of the antibody.
該アミラーゼに結合性の強い吸着体、即ち不溶性の担
体として、好ましいのは澱粉である。この吸着体の形態
としては、粉末、ディスク、濾紙、カラム等自由に成形
したものを用いることができる。Starch is preferred as an adsorbent having a strong binding to the amylase, that is, an insoluble carrier. As the form of the adsorbent, a freely formed one such as powder, disk, filter paper, and column can be used.
本発明の非アミラーゼ標識抗体及びアミラーゼ標識抗
体に用いる抗体は、モノクロナール抗体、またはポリク
ロナール抗体を問わず使用できる。また、モノクロナー
ル抗体とポリクロナール抗体を組み合わせてもよい。好
ましくは、エピトープの異なる抗体を用いることが望ま
しい。The antibody used for the non-amylase-labeled antibody and the amylase-labeled antibody of the present invention can be used regardless of whether it is a monoclonal antibody or a polyclonal antibody. Further, a monoclonal antibody and a polyclonal antibody may be combined. Preferably, it is desirable to use antibodies having different epitopes.
本発明のアミラーゼとしては、α−アミラーゼ、β−
アミラーゼ、グルコアミラーゼ、タカアミラーゼ等の各
種のアミラーゼを用いることができる。本発明におい
て、安定性や澱粉に対する吸着性のよい微生物由来のBa
cillus aubtilis （液化型）が好ましい。As the amylase of the present invention, α-amylase, β-amylase
Various amylases such as amylase, glucoamylase and Taka amylase can be used. In the present invention, a microorganism-derived Ba having good stability and adsorptivity to starch
Cillus aubtilis (liquefied) is preferred.
さらに、アミラーゼの吸着体に利用する澱粉にはトウ
モロコシ、小麦、米、ジャガイモ、サツマイモ等のもの
が使用できる。これら澱粉の吸着性は、加圧加熱法や加
熱法により増強させることができる。Further, as the starch used for the amylase adsorbent, corn, wheat, rice, potato, sweet potato and the like can be used. The adsorptivity of these starches can be enhanced by a pressure heating method or a heating method.
非アミラーゼ標識抗体に用いる標識物質にはアミラー
ゼ以外の酵素、蛍光物質、発光物質、放射性物質、補酵
素、ビオチン、アビジン、ストレプトアビジン、磁性物
質等の直接、間接的に測定可能な検知物質であれば使用
可能である。The labeling substance used for the non-amylase-labeled antibody may be an enzyme other than amylase, a fluorescent substance, a luminescent substance, a radioactive substance, a coenzyme, a biotin, avidin, streptavidin, a magnetic substance, or any other detectable substance that can be measured directly or indirectly. Can be used.
（作用） 抗原又は抗体の測定方法の態様について以下に述べ
る。(Action) An embodiment of a method for measuring an antigen or an antibody will be described below.
抗原の測定 試料中の抗原に、特異的な非アミラーゼ標識抗体とア
ミラーゼ標識抗体を加え、一定時間抗原抗体反応を行わ
せた後、この反応液をアミラーゼ結合性の吸着体に接触
又は通過させる。ついで、洗浄によって残存の非アミラ
ーゼ標識抗体を除去し、B/F分離を行い、抗原抗体反応
を起こした非アミラーゼ標識抗体の標識活性を測定す
る。Measurement of Antigen A specific non-amylase-labeled antibody and an amylase-labeled antibody are added to the antigen in the sample, and the antigen-antibody reaction is performed for a certain period of time. Then, the reaction solution is contacted or passed through an amylase-binding adsorbent. Next, the remaining non-amylase-labeled antibody is removed by washing, B / F separation is performed, and the labeling activity of the non-amylase-labeled antibody that has caused an antigen-antibody reaction is measured.
試料中の抗原に非アミラーゼ標識抗原とアミラーゼ標
識抗体を加え、一定時間抗原抗体反応を行わせた後、こ
の反応液をアミラーゼ結合性の吸着体に接触又は通過さ
せる。ついで、洗浄によって残存の非アミラーゼ標識抗
原を除去し、B/F分離を行い、抗原抗体反応を起こした
非アミラーゼ標識抗原の標識活性を測定する。After adding a non-amylase-labeled antigen and an amylase-labeled antibody to the antigen in the sample and allowing the antigen-antibody reaction to proceed for a certain period of time, the reaction solution is contacted or passed through an amylase-binding adsorbent. Next, the remaining non-amylase-labeled antigen is removed by washing, B / F separation is performed, and the labeling activity of the non-amylase-labeled antigen that has caused an antigen-antibody reaction is measured.
抗体の測定 試料中の抗体に、特異的な非アミラーゼ標識抗原とア
ミラーゼ標識抗原を加え、一定時間抗原抗体反応を行わ
せた後、この反応液をアミラーゼ結合性の吸着体に接触
又は通過させる。ついで、洗浄によって残存の非アミラ
ーゼ標識抗原を除去し、B/F分離を行い、抗原抗体反応
を起こした非アミラーゼ標識抗原の標識活性を測定す
る。Measurement of Antibody A specific non-amylase-labeled antigen and an amylase-labeled antigen are added to the antibody in the sample, and an antigen-antibody reaction is performed for a certain period of time. Then, the reaction solution is contacted or passed through an amylase-binding adsorbent. Next, the remaining non-amylase-labeled antigen is removed by washing, B / F separation is performed, and the labeling activity of the non-amylase-labeled antigen that has caused an antigen-antibody reaction is measured.
試料中の抗体に非アミラーゼ標識抗体とアミラーゼ標
識抗原を加え、一定時間抗原抗体反応を行わせた後、こ
の反応液をアミラーゼ結合性の吸着体に接触又は通過さ
せる。ついで、洗浄によって残存の非アミラーゼ標識抗
体を除去し、B/F分離を行い、抗原抗体反応を起こした
非アミラーゼ標識抗体の標識活性を測定する。A non-amylase-labeled antibody and an amylase-labeled antigen are added to the antibody in the sample, and after an antigen-antibody reaction is performed for a certain period of time, the reaction solution is brought into contact with or passed through an amylase-binding adsorbent. Next, the remaining non-amylase-labeled antibody is removed by washing, B / F separation is performed, and the labeling activity of the non-amylase-labeled antibody that has caused an antigen-antibody reaction is measured.
（実施例） 以下に実施例を挙げて本発明をさらに具体的に説明す
る。(Example) Hereinafter, the present invention will be described more specifically with reference to examples.
試薬 抗原（CEA）の各種濃度の標準液（0,2.5,5,10,20,40,
80 ng/ml） アミラーゼ標識抗体 ペルオキシダーゼ標識抗体 トウモロコシ澱粉 基質液（50mMクエン酸緩衝液、5mM過酸化水素、10mM
オルトフェニレンジアミン、pH5） 停止液（4N硫酸） 操作方法 試験管に各種濃度の標準液又は検体100μｌとアミラ
ーゼ標識抗体及びペルオキシダーゼ標識抗体各200μｌ
づつ加え37℃10分間反応させる。Reagent Antigen (CEA) standard solution (0,2.5,5,10,20,40,
Amylase-labeled antibody Peroxidase-labeled antibody Maize starch substrate solution (50 mM citrate buffer, 5 mM hydrogen peroxide, 10 mM
Orthophenylenediamine, pH5) Stop solution (4N sulfuric acid) Procedure 100 μl of standard solution or sample of various concentrations in test tube, 200 μl of amylase-labeled antibody and peroxidase-labeled antibody
Add at 37 ° C for 10 minutes.
反応液にトウモロコシ澱粉20mgを加え37℃10分間吸着
させる。20 mg of corn starch is added to the reaction solution, and adsorbed at 37 ° C. for 10 minutes.
2000G以上で１分間遠心後上澄みを捨てる。Discard the supernatant after centrifugation at 2000G or more for 1 minute.
洗浄液（生理食塩水）1mlで３回洗浄する。Wash 3 times with 1 ml of washing solution (physiological saline).
沈渣に基質液500μｌを加え、37℃30分間反応後停止
液200μｌを加える。Add 500 μl of substrate solution to the sediment, add 200 μl of stop solution after reaction at 37 ° C. for 30 minutes.
2000G以上で１分間遠心後上澄み200μｌをマイクロプ
レートに移し、マイクロプレートリーダーで波長492/63
0nmで吸光度を測定する。After centrifugation at 2,000 G or more for 1 minute, transfer 200 μl of the supernatant to a microplate, and use a microplate reader for wavelength 492/63.
Measure absorbance at 0 nm.
結果 CEA濃度80ng/ml以下で良好な検量線が得られた（第１
図）。Results A good calibration curve was obtained at a CEA concentration of 80 ng / ml or less (No. 1).
Figure).
実施例２ 実施例１と同様の試薬を用い、澱粉充填カラムによる
B/F分離を行った場合を説明する。Example 2 Using the same reagent as in Example 1, using a starch-filled column
The case where B / F separation is performed will be described.
操作方法 試験管にCEA濃度０と80ng/mlの標準液100μｌとアミ
ラーゼ標識抗体及びペルオキシダーゼ標識抗体各200μ
ｌづつ加え37℃10分間反応させる。Procedure 100 μl of standard solution with CEA concentration of 0 and 80 ng / ml, amylase-labeled antibody and peroxidase-labeled antibody 200 μl each in a test tube
The reaction was continued at 37 ° C for 10 minutes.
反応液をトウモロコシ澱粉20mg充填カラムに流し吸着
させる。The reaction solution is passed through a column packed with 20 mg of corn starch to be adsorbed.
洗浄液（生理食塩水）5mlを流し洗浄する。Wash with 5 ml of washing solution (physiological saline).
カラムの下方をコックで止める。Stop the lower part of the column with a cock.
カラムに基質液500μｌを加え反応させる。500 μl of the substrate solution is added to the column and reacted.
発色の強さを目視判定する。The intensity of coloring is visually determined.
結果 CEA80ng/mlのものは強く黄色に発色しCEA濃度０と80n
g/mlとの間に有意な差があった。Results CEA 80 ng / ml strongly developed yellow color and CEA concentration 0 and 80 n
g / ml.
以上のように、本発明によれば、抗原抗体反応時にお
いて被層での反応が可能であることにより反応時間が短
縮でき、試料中の微量成分と抗原抗体反応によって生じ
たアミラーゼ標識抗体−抗原−標識抗体の抗原抗体反応
複合物をアミラーゼを介して澱粉等の吸着体に吸着して
B/F分離を容易かつ迅速に行い、当該微量成分を極めて
効率的に測定できるという効果が達成される。As described above, according to the present invention, a reaction time can be shortened by allowing a reaction in a layer at the time of an antigen-antibody reaction, and a trace component in a sample and an amylase-labeled antibody-antigen generated by the antigen-antibody reaction -The antigen-antibody reaction complex of the labeled antibody is adsorbed to an adsorbent such as starch via amylase.
The effect that B / F separation is easily and quickly performed, and the trace component can be measured very efficiently is achieved.
第１図は実施例１によって得た検量線を示すグラフであ
る。FIG. 1 is a graph showing a calibration curve obtained in Example 1.
Claims (6)
な非アミラーゼ標識抗体とアミラーゼ標識抗体を反応さ
せた後、アミラーゼに結合性の強い吸着体によりB/F分
離を行い該吸着体に吸着した非アミラーゼ標識抗体の標
識活性により試料中の抗原を測定することを特徴とする
免疫学的測定方法。In a homogeneous liquid phase system, a non-amylase-labeled antibody specific to an antigen in a sample is allowed to react with an amylase-labeled antibody, followed by B / F separation using an adsorbent having a strong binding to amylase. An immunoassay method comprising measuring an antigen in a sample by a labeling activity of a non-amylase-labeled antibody adsorbed on a sample.
な非アミラーゼ標識抗原とアミラーゼ標識抗原を反応さ
せた後、アミラーゼに結合性の強い吸着体によりB/F分
離を行い該吸着体に吸着した非アミラーゼ標識抗原の標
識活性により試料中の抗体を測定することを特徴とする
免疫学的測定方法。2. A reaction between a non-amylase-labeled antigen specific to an antibody in a sample and an amylase-labeled antigen in a homogeneous liquid phase system, followed by B / F separation using an adsorbent having a strong binding to amylase, An immunoassay method comprising measuring an antibody in a sample by a labeling activity of a non-amylase-labeled antigen adsorbed on a sample.
る非アミラーゼ標識抗原とアミラーゼ標識抗体を反応さ
せた後、アミラーゼに結合性の強い吸着体によりB/F分
離を行い該吸着体に吸着した非アミラーゼ標識抗原の標
識活性により試料中の抗原を測定することを特徴とする
免疫学的測定方法。3. After reacting a non-amylase-labeled antigen and an amylase-labeled antibody that compete with an antigen in a sample in a liquid phase homogeneous system, B / F separation is carried out using an adsorbent having a strong binding to amylase, and the adsorbent is subjected to B / F separation. An immunoassay method comprising measuring an antigen in a sample by a labeling activity of an adsorbed non-amylase-labeled antigen.
る非アミラーゼ標識抗体とアミラーゼ標識抗原を反応さ
せた後、アミラーゼに結合性の強い吸着体によりB/F分
離を行い該吸着体に吸着した非アミラーゼ標識抗体の標
識活性により試料中の抗体を測定することを特徴とする
免疫学的測定方法。4. After reacting a non-amylase-labeled antibody and an amylase-labeled antigen which compete with an antibody in a sample in a liquid phase homogeneous system, B / F separation is carried out with an adsorbent having a strong binding to amylase, and the adsorbent is subjected to B / F separation. An immunoassay method comprising measuring an antibody in a sample based on the labeling activity of the adsorbed non-amylase-labeled antibody.
粉であることを特徴とする請求項（１）〜（４）のいず
れか１項記載の免疫学的測定方法。5. The immunological assay method according to claim 1, wherein the adsorbent having a strong binding property to amylase is starch.
際、標識がアミラーゼ以外の酵素であることを特徴とす
る請求項（１）〜（５）のいずれか１項記載の免疫学的
測定方法。6. The immunoassay according to claim 1, wherein when using a non-amylase-labeled antigen or antibody, the label is an enzyme other than amylase.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP1150743A JP2714143B2 (en) | 1989-06-14 | 1989-06-14 | Immunological measurement method |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP1150743A JP2714143B2 (en) | 1989-06-14 | 1989-06-14 | Immunological measurement method |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH0315759A JPH0315759A (en) | 1991-01-24 |
| JP2714143B2 true JP2714143B2 (en) | 1998-02-16 |
Family
ID=15503448
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP1150743A Expired - Fee Related JP2714143B2 (en) | 1989-06-14 | 1989-06-14 | Immunological measurement method |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JP2714143B2 (en) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP5090100B2 (en) | 2007-08-09 | 2012-12-05 | 豊田合成株式会社 | Inflator |
| JP4332189B2 (en) | 2007-08-09 | 2009-09-16 | トヨタ自動車株式会社 | Inflator and vehicle airbag apparatus using the same |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB8307156D0 (en) * | 1983-03-15 | 1983-04-20 | Celltech Ltd | Heterogeneous binding assays |
| JPS6339895A (en) * | 1986-05-15 | 1988-02-20 | イ−・アイ・デユポン・ド・ネモア−ス・アンド・コンパニ− | Bioaffinity and ion exchange separation using liquid support |
-
1989
- 1989-06-14 JP JP1150743A patent/JP2714143B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| JPH0315759A (en) | 1991-01-24 |
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