JPH01285857A - Invitro measurement for density of analysis material - Google Patents
Invitro measurement for density of analysis materialInfo
- Publication number
- JPH01285857A JPH01285857A JP9843688A JP9843688A JPH01285857A JP H01285857 A JPH01285857 A JP H01285857A JP 9843688 A JP9843688 A JP 9843688A JP 9843688 A JP9843688 A JP 9843688A JP H01285857 A JPH01285857 A JP H01285857A
- Authority
- JP
- Japan
- Prior art keywords
- antigen
- labeled
- antibody
- analyte
- equilibrium reaction
- 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
- 238000004458 analytical method Methods 0.000 title description 2
- 238000005259 measurement Methods 0.000 title 1
- 239000000427 antigen Substances 0.000 claims abstract description 49
- 102000036639 antigens Human genes 0.000 claims abstract description 46
- 108091007433 antigens Proteins 0.000 claims abstract description 46
- 238000000034 method Methods 0.000 claims abstract description 24
- 238000006243 chemical reaction Methods 0.000 claims abstract description 22
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 12
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 12
- 239000007790 solid phase Substances 0.000 claims abstract description 8
- 230000002401 inhibitory effect Effects 0.000 claims abstract description 5
- 239000000376 reactant Substances 0.000 claims description 16
- 239000012491 analyte Substances 0.000 claims description 14
- 230000027455 binding Effects 0.000 claims description 6
- 239000007787 solid Substances 0.000 claims description 5
- 239000012071 phase Substances 0.000 claims description 4
- 108010032595 Antibody Binding Sites Proteins 0.000 claims description 3
- 238000000338 in vitro Methods 0.000 claims description 3
- 230000000903 blocking effect Effects 0.000 claims description 2
- 239000000126 substance Substances 0.000 abstract description 5
- 230000035945 sensitivity Effects 0.000 abstract description 4
- 239000000203 mixture Substances 0.000 abstract description 2
- 238000012875 competitive assay Methods 0.000 description 5
- 238000011067 equilibration Methods 0.000 description 5
- 102000011923 Thyrotropin Human genes 0.000 description 3
- 108010061174 Thyrotropin Proteins 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 239000011230 binding agent Substances 0.000 description 3
- 238000010494 dissociation reaction Methods 0.000 description 3
- 230000005593 dissociations Effects 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 101710098119 Chaperonin GroEL 2 Proteins 0.000 description 2
- 230000003100 immobilizing effect Effects 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 101100258233 Caenorhabditis elegans sun-1 gene Proteins 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 238000010420 art technique Methods 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 230000009918 complex formation Effects 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 239000003292 glue Substances 0.000 description 1
- 238000003365 immunocytochemistry Methods 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 238000000670 ligand binding assay Methods 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
Landscapes
- Investigating Or Analysing Biological Materials (AREA)
Abstract
Description
【発明の詳細な説明】
（産業上の利用分野）
本発明は、例えば、血中のチオキシン（Ｔ ４ ）、イ
ノン−＋、 １．１ンおよび甲状腺刺激ホルモン等のイ
ンビトロ分析を目的とするりガンｌ″結合アッセイにお
ける分析物質濃度の測定方法に関するものであン）。DETAILED DESCRIPTION OF THE INVENTION (Field of Industrial Application) The present invention is useful for in vitro analysis of thioxine (T4), ynone-+, 1.1-tin, thyroid stimulating hormone, etc. in blood. A method for measuring the concentration of an analyte in a binding assay.
（従来の技術とその課題）
競合結合アッセイおよびサントイノチア、セイ技術を含
むリガンド結合アッセイ技術によって分析物質濃度を測
定することが知られている。競合結合アッセイの一形態
として、例えば、抗原Ａのような測定すべき反応物質を
既知濃度のラベル化した反応物質と抗原へに対する抗体
のようなバインダーと共にインキュベートし、ラベル化
および非う−・ル化抗原をバインダーの結合部位に対し
て競合させる。この結合した抗原−抗体複合体を遊離ラ
ベル化および非ラヘル化抗原から分離し、結合しまた該
複合体からの情報が分析物質濃度を見積るための非ラヘ
ル化抗原Ａとの数学的関係をもたらす。BACKGROUND OF THE INVENTION It is known to measure analyte concentration by ligand binding assay techniques, including competitive binding assays and Santoinotia and Sei techniques. In one form of competitive binding assay, a reactant to be measured, e.g. antigen A, is incubated with a known concentration of labeled reactant and a binder, such as an antibody to the antigen. conjugated antigen competes for binding sites on the binder. This bound antigen-antibody complex is separated from free labeled and non-Lahelized antigen, and the information from the complex provides a mathematical relationship with non-Lahelized antigen A for estimating the analyte concentration. .
一般に、分離はプラスチックチューブ、ビーズまたは不
活性化粒子のような固相上に抗体を不動化することによ
って、あるいは複合体を沈澱させることによって実施さ
れる。Generally, separation is performed by immobilizing the antibody on a solid phase such as plastic tubes, beads or inactivated particles, or by precipitating the complex.
サン１〜・イノチア、セイ技術においては、抗原［もの
ような測定すべき反応物質は、継続的または同時に他の
既知濃度のラベル化反応物質、例えばラベル化抗Ｂ抗体
に、既知濃度の非うヘル化ハ・インダー過剰に対して添
加し、抗体−抗原 ラベル化抗体サン１−インチ複合体
を形成するものである。In San1~ Inochia and Sei technology, a reactive substance to be measured, such as an antigen, is continuously or simultaneously added to a known concentration of a labeled reactive substance, such as a labeled anti-B antibody. The antibody is added to an excess of conjugated antibody to form an antibody-antigen labeled antibody complex.
、−の複合体と過剰抗体は＋！！！離抗原と遊１Ｔｉｌ
ｉ’Ｔｊヘル化抗体から分離されるが、通常、反応前不
活化同相十〇こ非ラベル化抗体を不動化することによっ
て、該サンドイッチ複合体は例えばデカンデージョンに
よって物理的に分離される。該サン１イ、千復合体から
の情報が分析物質濃度を見積るための非ラヘル化抗原Ｂ
との数学的関係をもたらす。, - complex and excess antibody are +! ! ! Free antigen and free 1Til
The sandwich complex is physically separated, eg, by decandation, by immobilizing the unlabeled antibody, which is separated from the i'Tj antibody, but is usually inactivated prior to reaction. The information from the San 1, 1,000 conjugate is used to estimate the analyte concentration.
brings about a mathematical relationship with.
上記競合結合アッセイ技術は、チし］キシン（１゛４）
の測定に用いられ、該サン１イノチアノセイ技術は甲状
腺刺激ホルモン（ＴＳＨ）およびインシュリンの測定に
用いられる。The competitive binding assay technique described above is based on thioxyxin (1゛4).
The Sun 1 Inocyanosis technique is used to measure thyroid stimulating hormone (TSH) and insulin.
公知技術において、反応性抗原と反応性抗体の繰返し、
再接触が反応物質とバインダーとの平衡を達成するため
用いられＴいるが、これは分析物質を疲労させる原因と
なる。該サンドイッチアッセイ技術において、更に不利
な点は、結合された抗原が解離し易く、その結果、該サ
ンドイッチ複合体を形成するだめの、シ・へ・ル化抗体
の該結合された抗原への結合を阻害する。引き続いて反
応物質の添加が行われると、不動化サントイ、チ複合体
から結合した抗原−ラベル化抗体の一部が解離する。抗
原濃度が増加するに従って、該阻害あるいは解離の程度
が増大し、その結果アッセイを不正確にした。該阻害ま
たは解離の影響は「フック効果」として知られている。In the known technology, repeating reactive antigen and reactive antibody,
Recontact is used to achieve equilibrium between reactants and binder, but this causes fatigue of the analyte. A further disadvantage in the sandwich assay technique is that the bound antigen is likely to dissociate, resulting in the binding of the bound antigen to the bound antigen without forming the sandwich complex. inhibit. Subsequent addition of the reactant causes a portion of the bound antigen-labeled antibody to dissociate from the immobilized Santoy, Chi complex. As the antigen concentration increased, the degree of inhibition or dissociation increased, making the assay inaccurate. This inhibition or dissociation effect is known as the "hook effect".
本発明の目的は、公知のりガンｌ：結合アソセ・イ技術
の感度を増大することである。It is an object of the present invention to increase the sensitivity of known glue gun/bonding assembly techniques.
（課題を解決するだめの手段）
本発明１こよれば、我々は、測定すべき分析物質と固相
担体上に不動化された反応物質との平衡反応からなる方
法であって、不動化された反応物質部位の幾−つかと共
に、該固相担体上に存在する活性部位が平衡反応以前、
蛋白質により阻害されていることを特徴とする分析物質
濃度のインビトロ測定方法を提供する。(Means for Solving the Problems) According to the present invention 1, we have provided a method consisting of an equilibrium reaction between an analyte to be measured and a reactant immobilized on a solid phase support. Before the equilibrium reaction, the active sites present on the solid support, together with some of the reactant sites
Provided is an in vitro method for measuring the concentration of an analyte, characterized in that it is inhibited by a protein.
競合結合アッセイ技術に適用される本発明は、ラベル化
抗原と非ラヘル化抗原による反応以前に抗体の結合部位
の幾つかと共に該固相担体上に存在する活性部位を阻害
すること、および該平衡反応後、不結合のラベル化抗原
および非ラヘル化抗原を捨てることからなる方法である
。The present invention, applied to competitive binding assay techniques, involves inhibiting the active sites present on the solid support along with some of the binding sites of the antibody prior to the reaction between the labeled antigen and the non-Lachelated antigen, and the equilibrium After the reaction, the method consists of discarding unbound labeled antigen and non-Rahelized antigen.
該ザンｌイノチアノセイ技術に適用される本発明は、ラ
ベル化抗体と非ラヘル化抗原による反応以前に非ラベル
化抗体の結合部位の幾つかと共に該同相担体上に存在す
る活性部位を阻害すること、および該平衡反応後、不結
合のラベル化抗体および非ラヘル化抗原を捨てることか
らなる方法である。The present invention applied to the X-ray inocyanase technology involves inhibiting the active site present on the homologous carrier together with some of the binding sites of the unlabeled antibody prior to the reaction between the labeled antibody and the non-labeled antigen; and after the equilibrium reaction, the unbound labeled antibody and non-Raherized antigen are discarded.
繰返される再平衡が反応物質の疲労は引き起こした従来
技術に比べて本発明が便利な点は新鮮な反応物質による
再平衡が実施され、その結果、アッセイの感度が少なく
とも３つの因子による各々の再平衡により増大する。特
に、本発明方法は分析物質濃度を維持し、かつ、サン１
イノチアノセイ技術において不動化サンドイッチ複合体
からの結合した抗原（引き続き反応物質が添加される場
合）または抗原−ラベル化抗体の一部（反応物質の同時
添加が用いられる場合）の解離が減少するの−〔、−ア
、・２り効果の発現を防しトする。An advantage of the present invention compared to prior art techniques in which repeated re-equilibrations caused fatigue of the reactants is that re-equilibrations with fresh reactants are performed, so that the sensitivity of the assay is reduced by at least three factors with each re-equilibration. Increases due to equilibrium. In particular, the method of the invention maintains analyte concentration and
The dissociation of bound antigen (if subsequent addition of reactant is used) or part of the antigen-labeled antibody (if simultaneous addition of reactant is used) from the immobilized sandwich complex in the immunocytochemistry technique is reduced. [,-A, ・Prevent the expression of the second effect.
本発明の々仁ｔしい態様は、測定′４−べき新鮮な反応
′Ｉ′）Ｊ質か初めの平復１及応の結果として該同相担
体トにｉ７合づる反蛇、・物ＴＩと、％貫）ｊ１嘘１．
ど共に再５１ノｉ動化される時、反応物質部位を阻害し
ている蛋白質の幾つかめ補！１定−１−＼き分＋Ｉ’■
’４！／ｌ質に置き換えらｒｈることにより結合された
複合体からの情報が測定すべき分析物質濃度に一層正確
に関連する方法である。A very benign embodiment of the present invention is to measure a fresh reaction 'I') which is combined with the in-phase carrier as a result of the initial reaction. % kan) j1 lie 1.
When re-activated, some of the proteins blocking the reactant site will be removed! 1 constant - 1 - \ki minute + I'■
'4! By replacing the /l substance with rh, the information from the combined complexes is more accurately related to the analyte concentration to be measured.
以下、添イ」図面を参照し、て本発明の詳細な説明する
。Hereinafter, the present invention will be described in detail with reference to the accompanying drawings.
初めに、第１図（、］）において、初めの平衡反応を示
した。新鮮なラベル化抗原およびノ１ラベル化抗厚は固
相（り体上乙こ不動化された抗体と反応Ｊるが、この時
、抗体結合部位の幾つかと共に同相担体−１−に残存す
る活性部位は阻害されている状態である。ラベル化抗原
およびＪｌ−：）ヘル化抗原は阻害されていない結合部
位に対して競合する。First, the initial equilibrium reaction is shown in Figure 1 (, ]). The freshly labeled antigen and the labeled antibody react with the immobilized antibody on the solid phase, leaving some of the antibody binding sites on the carrier. The active site is in the inhibited state. Labeled antigen and Jl-:)Helved antigen compete for the uninhibited binding site.
ＭＭ （結合していない）ラヘル化抗原および、（ＩＥ
ラヘル化抗原は捨てられる。第１図（ｂ）に示した再平
衡反応において、新鮮なラヘル化抗原お主反応され、蛋
白質分子の幾つかは抗原により置き換えられ、ラベル化
抗原および、Ｊｌ−ラ・・、ル化抗原の総量は、反応物
質混合物の量に比例して・層正確になる。MM (unbound) Rahelized antigen and (IE
Rahelized antigens are discarded. In the re-equilibration reaction shown in Figure 1(b), the fresh labeled antigen is mainly reacted, some of the protein molecules are replaced by the antigen, and the labeled antigen and the labeled antigen are The total amount is proportional to the amount of reactant mixture.
遊離のラベル化および非ラベル化抗原は置換された蛋白
質と共に捨てられる。Free labeled and unlabeled antigen are discarded along with the displaced protein.
第２図（４１）は、４Ｊントイノ千ア、セイ平衡反応を
示し２、新鮮なラベル化抗体とＪＶラヘル化抗原が同相
担体上に不動化された非ラヘル化抗体と反応するが、こ
の時、抗体結合部位の幾つかと共に同相担体上に残存す
る活性部位は阻害されている状態である。非ラベル化抗
体−抗原 ラベル化抗体ザン（・イノチ複合体が阻害さ
れていない非ラベル化抗体部位に形成される。遊離（結
合していない）ラベル化抗体と非ラヘル化抗原は捨てら
れる。Figure 2 (41) shows the 4J toinochia-Sei equilibrium reaction 2, in which freshly labeled antibodies and JV Lachelated antigens react with non-Lachelated antibodies immobilized on the same phase carrier. , the active site remaining on the co-phase carrier along with some of the antibody binding sites is in a blocked state. Unlabeled antibody-antigen Labeled antibody-antigen complexes are formed at uninhibited unlabeled antibody sites. Free (unbound) labeled antibody and non-labeled antigen are discarded.
第２図（＋））に示した再平衡反応において、新ｂ′（
なラベル化抗体と非ラヘル化抗原は更に」−記不動化さ
れた抗体と反応され、蛋白質分子の幾つかは追加される
複合体形成を４１容するために置き換えられる。In the re-equilibration reaction shown in Figure 2 (+)), the new b'(
The labeled antibody and non-Rachelated antigen are further reacted with the immobilized antibody and some of the protein molecules are replaced to allow for additional complex formation.
遊離のラベル化抗体および非ラヘル化抗原は置換された
蛋白質と共に捨てられる。Free labeled antibody and non-Rachelized antigen are discarded along with the displaced protein.
第１図（ａ）および（ｂ）は競合結合ア・７セイ技術に
適用される本発明法を図式的に説明するｌであり、第２
図（ａ）および（ｂ）は１ナン］・イノチアンセイ技術
に適用される本発明法を図式的に説明する図である。
○ ： 蛋白質
＼″′： 非ラヘル化抗体
■
す１ ： ラベル化抗体
＼
−： 固相担体
代理人弁理士（８１０７）佐々木 清除（ほか３名）
手続補正書
昭和６３年７月２２日Figures 1(a) and (b) schematically illustrate the method of the present invention applied to competitive binding assay technology;
Figures (a) and (b) are diagrams schematically illustrating the method of the present invention applied to the 1nan]-inochianse technique. ○: Protein ＼″′: Non-Lachelated antibody■ Su1: Labeled antibody＼ -: Solid phase carrier representative patent attorney (8107) Seiyoshi Sasaki (and 3 others) Procedural amendment July 22, 1988
Claims (1)
応物質との平衡反応からなる方法であって、不動化され
た反応物質部位の幾つかと共に、該固相担体上に存在す
る活性部位が平衡反応以前、蛋白質により阻害されてい
ることを特徴とする分析物質濃度のインビトロ測定方法
。 ２、ラベル化抗原と非ラベル化抗原による反応以前に抗
体の結合部位の幾つかと共に該固相担体上に存在する活
性部位を阻害すること、および該平衡反応後、不結合の
ラベル化抗原および非ラベル化抗原を捨てることを特徴
とする請求項１記載の方法。 ３、ラベル化抗体と非ラベル化抗原による反応以前に非
ラベル化抗体の結合部位の幾つかと共に該固相担体上に
存在する活性部位を阻害すること、および該平衡反応後
、不結合のラベル化抗体および非ラベル化抗原を捨てる
ことを特徴とする請求項１記載の方法。 ４、測定すべき新鮮な反応物質が初めの平衡反応の結果
として該固相担体上に存在する反応物質と分析物質と共
に再平衡化される時、反応物質部位を阻害している蛋白
質の幾つかが測定すべき分析物質に置き換えられること
により結合された複合体からの情報が測定すべき分析物
質濃度に一層正確に関連することを特徴とする請求項１
〜３の何れか１項に記載の方法。 ５、後記および添付図面で説明されている方法。[Scope of Claims] 1. A method consisting of an equilibrium reaction between an analyte to be measured and a reactant immobilized on a solid support, the method comprising: An in vitro method for measuring the concentration of an analyte, characterized in that active sites present on a phase carrier are inhibited by a protein before equilibrium reaction. 2. inhibiting the active site present on the solid support along with some of the antibody binding sites before the reaction between labeled and unlabeled antigen; and after the equilibrium reaction, unbound labeled antigen and 2. A method according to claim 1, characterized in that unlabeled antigen is discarded. 3. Inhibiting the active site present on the solid support together with some of the binding sites of the unlabeled antibody before the reaction between the labeled antibody and the unlabeled antigen, and after the equilibrium reaction, the unbound label 2. A method according to claim 1, characterized in that labeled antibodies and unlabeled antigens are discarded. 4. When the fresh reactant to be measured is re-equilibrated with the reactant and analyte present on the solid phase support as a result of the initial equilibrium reaction, some of the proteins blocking the reactant site are is replaced by the analyte to be measured, so that the information from the combined complex relates more precisely to the analyte concentration to be measured.
3. The method according to any one of items 3 to 3. 5. The method described below and in the accompanying drawings.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP9843688A JPH01285857A (en) | 1988-04-22 | 1988-04-22 | Invitro measurement for density of analysis material |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP9843688A JPH01285857A (en) | 1988-04-22 | 1988-04-22 | Invitro measurement for density of analysis material |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH01285857A true JPH01285857A (en) | 1989-11-16 |
Family
ID=14219737
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP9843688A Pending JPH01285857A (en) | 1988-04-22 | 1988-04-22 | Invitro measurement for density of analysis material |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH01285857A (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2002365298A (en) * | 2001-06-08 | 2002-12-18 | Tosoh Corp | Measurement inhibition reducing method and reagent composition |
| JP2007024498A (en) * | 2005-07-12 | 2007-02-01 | Rohm Co Ltd | Immunoassay method and biochip |
-
1988
- 1988-04-22 JP JP9843688A patent/JPH01285857A/en active Pending
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2002365298A (en) * | 2001-06-08 | 2002-12-18 | Tosoh Corp | Measurement inhibition reducing method and reagent composition |
| JP2007024498A (en) * | 2005-07-12 | 2007-02-01 | Rohm Co Ltd | Immunoassay method and biochip |
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