JPH0531743B2 - - Google Patents
Info
- Publication number
- JPH0531743B2 JPH0531743B2 JP59047924A JP4792484A JPH0531743B2 JP H0531743 B2 JPH0531743 B2 JP H0531743B2 JP 59047924 A JP59047924 A JP 59047924A JP 4792484 A JP4792484 A JP 4792484A JP H0531743 B2 JPH0531743 B2 JP H0531743B2
- Authority
- JP
- Japan
- Prior art keywords
- peroxidase
- labeled anti
- igg
- human
- phenol
- 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.)
- Expired - Lifetime
Links
- 102000013415 peroxidase activity proteins Human genes 0.000 claims description 22
- 108040007629 peroxidase activity proteins Proteins 0.000 claims description 22
- 108091003079 Bovine Serum Albumin Proteins 0.000 claims description 11
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 claims description 11
- 229940098773 bovine serum albumin Drugs 0.000 claims description 11
- 239000007853 buffer solution Substances 0.000 claims description 7
- 239000000203 mixture Substances 0.000 claims description 3
- 239000000872 buffer Substances 0.000 claims description 2
- 239000011259 mixed solution Substances 0.000 claims 1
- 239000008363 phosphate buffer Substances 0.000 description 7
- 102000004190 Enzymes Human genes 0.000 description 6
- 108090000790 Enzymes Proteins 0.000 description 6
- 238000005259 measurement Methods 0.000 description 6
- 230000000694 effects Effects 0.000 description 5
- 238000003018 immunoassay Methods 0.000 description 5
- 239000007788 liquid Substances 0.000 description 5
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 4
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 4
- 238000001514 detection method Methods 0.000 description 4
- 201000005404 rubella Diseases 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 210000002966 serum Anatomy 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- GEYOCULIXLDCMW-UHFFFAOYSA-N 1,2-phenylenediamine Chemical compound NC1=CC=CC=C1N GEYOCULIXLDCMW-UHFFFAOYSA-N 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
- 238000000034 method Methods 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 241000710799 Rubella virus Species 0.000 description 1
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 238000004737 colorimetric analysis Methods 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- ZBCBWPMODOFKDW-UHFFFAOYSA-N diethanolamine Chemical compound OCCNCCO ZBCBWPMODOFKDW-UHFFFAOYSA-N 0.000 description 1
- 230000008105 immune reaction Effects 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 230000003595 spectral effect Effects 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/531—Production of immunochemical test materials
- G01N33/532—Production of labelled immunochemicals
- G01N33/535—Production of labelled immunochemicals with enzyme label or co-enzymes, co-factors, enzyme inhibitors or enzyme substrates
Landscapes
- Health & Medical Sciences (AREA)
- Immunology (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Chemical & Material Sciences (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Cell Biology (AREA)
- Food Science & Technology (AREA)
- Medicinal Chemistry (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Description
【発明の詳細な説明】
本発明は抗原又は抗体などの免疫反応体の検出
及び測定特にエンザイムイムノアツセイに利用さ
れるパーオキシダーゼ標識抗ヒトIgG（γ）の液
状安定化のものを得んとするものである。なお、
前記パーオキシダーゼ標識抗ヒトIgG（γ）なる
記載においてIgGの後に括弧付きで示すγは、
IgGのＨ鎖がγ鎖であることを示している。DETAILED DESCRIPTION OF THE INVENTION The present invention aims to provide a liquid stabilized peroxidase-labeled anti-human IgG (γ) that can be used in the detection and measurement of immunoreactants such as antigens or antibodies, especially in enzyme immunoassays. It is something to do. In addition,
In the above description of peroxidase-labeled anti-human IgG (γ), γ shown in parentheses after IgG is:
This shows that the H chain of IgG is the γ chain.
一般にパーオキシダーゼ標識抗ヒトIgG（γ）
はこれを免疫学的検出法に応用することにより免
疫反応を酵素活性に由来する基質の色調変化によ
つて肉眼検出でき、更に比色法によつて定量的検
出も出来る有用な物質である。 Generally peroxidase-labeled anti-human IgG (γ)
By applying this to immunological detection methods, it is possible to detect immune reactions with the naked eye based on changes in the color tone of the substrate resulting from enzyme activity, and it is also a useful substance that can be quantitatively detected using a colorimetric method.
然しながらパーオキシダーゼ標識抗ヒトIgG
（γ）は液状とした場合、極めて不安定であり、
常温において放置すると分解をおこして使用でき
ないものとなる、従つて通常−20℃の如き低温度
にて凍結して保存しているものであるがこのよう
な温度に保存することはその使用並に貯蔵におい
て極めて困難な作業を要するものであり、パーオ
キシダーゼ標識抗ヒトIgG（γ）を使用した免疫
学的検出法の普及並に市場性において著しい制限
をうけているものである。 However, peroxidase-labeled anti-human IgG
(γ) is extremely unstable when it is in liquid form,
If left at room temperature, it will decompose and become unusable. Therefore, it is usually frozen and stored at a low temperature such as -20℃, but storing it at such a temperature may be harmful to its use. It requires extremely difficult storage operations, and is severely limiting its marketability and the spread of immunological detection methods using peroxidase-labeled anti-human IgG (γ).
本発明はかかる現状に鑑み鋭意研究を行つた結
果、パーオキシダーゼ標識抗ヒトIgG（γ）の液
状にした場合の安定化に成功したものである。即
ち本発明はパーオキシダーゼ標識抗ヒトIgG（γ）
に緩衝液とフエノール又は牛血清アルブミンの何
れか一方又は両者との混和液を添加したものであ
る。 The present invention has been made as a result of extensive research in view of the current situation, and has succeeded in stabilizing peroxidase-labeled anti-human IgG (γ) in liquid form. That is, the present invention provides peroxidase-labeled anti-human IgG (γ)
A mixture of a buffer solution and either or both of phenol and bovine serum albumin is added to the solution.
本発明において緩衝液に添加するフエノール又
は牛血清アルブミンの添加量において、フエノー
ルを0.1％以下又は牛血清アルブミン５％以下と
限定した理由は夫々の限定量を超えた場合には、
何れもパーオキシダーゼ標識抗ヒトIgG（γ）の
液状物が懸濁して蛋白が変質し使用にたえないも
のとなるためである。 In the present invention, the amount of phenol or bovine serum albumin added to the buffer solution is limited to 0.1% or less or bovine serum albumin to 5% or less.
In either case, the peroxidase-labeled anti-human IgG (γ) liquid becomes suspended and the protein is denatured, making it unusable.
なお緩衝液としてはトリス（ヒドロキシメチ
ル）アミノメタン、ジエタノール、トリエタノー
ル、リン酸、酢酸等を使用するものである。 As the buffer solution, tris(hydroxymethyl)aminomethane, diethanol, triethanol, phosphoric acid, acetic acid, etc. are used.
次に本発明の実施例について説明する。 Next, examples of the present invention will be described.
実施例 １
パーオキシダーゼ標識抗ヒトIgG（γ）に第１
表に示す如き緩衝液並に緩衝液にフエノール又は
牛血清アルブミンを添加し、これを500倍に希釈
した溶液を30℃に貯蔵した。Example 1 Peroxidase-labeled anti-human IgG (γ)
Buffer solutions as shown in the table and phenol or bovine serum albumin were added to the buffer solution and the solutions were diluted 500 times and stored at 30°C.
第 １ 表
比較例品(1) 5mMリン酸緩衝液（PH8.0）
本発明品(1) 0.01％フエノール入り5mMリン
酸緩衝液（PH8.0）
本発明品(2) １％牛血清アルブミン入り5mM
リン酸緩衝液（PH8.0）
本発明品(3) 0.01％フエノール及び１％牛血清
アルブミン入り5mMリン酸緩衝
液（PH8.0）
斯くして得た本発明品及び比較例品とについて
その性能を試みるために貯蔵日数とパーオキシダ
ーゼの活性度を測定した。なお活性度は30mMオ
ルトフエニレンジアミン0.02％過酸化水素共存下
に3N硫酸を添加し490nm／570nmにおける分光
度を測定したものである。その結果は第１図に示
す通りである。 Table 1 Comparative example product (1) 5mM phosphate buffer (PH8.0) Invention product (1) 5mM phosphate buffer containing 0.01% phenol (PH8.0) Invention product (2) 1% bovine serum albumin Contains 5mM
Phosphate buffer (PH8.0) Inventive product (3) 5mM phosphate buffer containing 0.01% phenol and 1% bovine serum albumin (PH8.0) Regarding the thus obtained inventive product and comparative example product. To test the performance, storage days and peroxidase activity were measured. The activity was determined by adding 3N sulfuric acid in the presence of 30mM orthophenylenediamine and 0.02% hydrogen peroxide, and measuring the spectroscopic intensity at 490nm/570nm. The results are shown in FIG.
第１図より明らかの如く本発明品は経時変化を
おこすことなく優れた安定性を示した。 As is clear from FIG. 1, the product of the present invention exhibited excellent stability without causing any change over time.
実施例 ２
パーオキシダーゼに0.01％フエノール及び１％
牛血清アルブミンと第２表に示す如く種々の緩衝
液との混和液を添加し、その溶液を30℃に貯蔵し
た。Example 2 Peroxidase with 0.01% phenol and 1%
A mixture of bovine serum albumin and various buffers as shown in Table 2 was added and the solution was stored at 30°C.
第 ２ 表
本発明品(3) 5mMリン酸緩衝液（PH8.0）
本発明品(4) 10mMトリス（ヒドロキシメチ
ル）アミノメタン（PH7.0）
本発明品(5) 10mMジエタノールアミン（PH
7.0）
本発明品(6) 10mMトリエタノールアミン（PH
7.0）
本発明品(7) 10mM酢酸緩衝液（PH5.0）
斯くして得た本発明品について実施例１と同様
にして貯蔵日数とパーオキシダーゼの活性度を測
定した。その結果は第２図に示す通りである。 Table 2 Invention product (3) 5mM phosphate buffer (PH8.0) Invention product (4) 10mM tris(hydroxymethyl)aminomethane (PH7.0) Invention product (5) 10mM diethanolamine (PH
7.0) Inventive product (6) 10mM triethanolamine (PH
7.0) Product of the present invention (7) 10mM acetate buffer (PH5.0) Regarding the thus obtained product of the present invention, storage days and peroxidase activity were measured in the same manner as in Example 1. The results are shown in FIG.
第２図より明らかの如く本発明品によれば何れ
の緩衝液を使用するものすべて優れた安定性を示
した。 As is clear from FIG. 2, the products of the present invention exhibited excellent stability regardless of the buffer solution used.
実施例 ３
パーオキシダーゼ標識抗ヒトIgG（γ）に0.01％
フエノール及び１％牛血清アルブミン入り5mM
リン酸緩衝液（PH8.0）を添加しこれを500倍に希
釈した本発明品についてこれをエンザイムイムノ
アツセイによる人血中風疹IgG抗体の測定に応用
し４℃における安定性を490nm／570nmの分光測
定により調べた。Example 3 0.01% peroxidase-labeled anti-human IgG (γ)
5mM with phenol and 1% bovine serum albumin
The product of the present invention, which was diluted 500 times by adding phosphate buffer (PH8.0), was applied to the measurement of rubella IgG antibodies in human blood by enzyme immunoassay, and the stability at 4°C was measured at 490nm/570nm. was investigated by spectroscopic measurements.
なおエンザイムイムノアツセイによる本発明パ
ーオキシダーゼ水溶液の他、風疹ウイルス固定マ
イクロプレート、30mMオルトフエニレンジアミ
ン、0.02％過酸化水素、3N硫酸を使用し人血清
として予研法によるHI価128の風疹抗体陽性人血
清を使用した。 In addition to the peroxidase aqueous solution of the present invention by enzyme immunoassay, rubella virus immobilized microplate, 30mM orthophenylenediamine, 0.02% hydrogen peroxide, and 3N sulfuric acid were used as human serum to test positive for rubella antibody with HI value of 128 by Yoken method. Human serum was used.
その結果は第３図に示す通りである。 The results are shown in FIG.
実施例 ４
パーオキシダーゼ標識抗ヒトIgG（γ）に0.01％
フエノール及び１％牛血清アルブミン入り5mM
リン酸緩衝液（PH8.0）を添加しこれを500倍に希
釈した本発明品をエンザイムイムノアツセイによ
る人血中風疹IgG抗体の測定に応用した。なおエ
ンザイムイムノアツセイによる風疹IgG抗体の測
定は実施例３に示す如く490nm／570nmの分光測
定により行つたものであり、人血清56例について
予研法によるHI価との相関性を検討し、本発明
品の免疫学的検出法の応用効果を調べた。Example 4 0.01% peroxidase-labeled anti-human IgG (γ)
5mM with phenol and 1% bovine serum albumin
The product of the present invention, which was diluted 500 times with the addition of phosphate buffer (PH8.0), was applied to the measurement of rubella IgG antibodies in human blood by enzyme immunoassay. The measurement of rubella IgG antibodies by enzyme immunoassay was performed by spectroscopic measurement at 490 nm/570 nm as shown in Example 3, and the correlation with the HI titer by Yoken method was examined for 56 human serum samples. The application effect of the invented immunological detection method was investigated.
その結果は第４図に示す通りである。 The results are shown in FIG.
以上詳述した如く本発明によればパーオキシダ
ーゼ標識抗ヒトIgG（γ）を液状のまま長期間安
心して保存することが出来るから抗原や抗体の免
疫反応体の検出及び測定に極めて有用に利用する
ことが出来る。 As detailed above, according to the present invention, peroxidase-labeled anti-human IgG (γ) can be safely stored in liquid form for a long period of time, making it extremely useful for detecting and measuring immunoreactants of antigens and antibodies. I can do it.
第１図乃至第４図は本発明安定化パーオキシダ
ーゼ標識抗ヒトIgG（γ）の性能を示すものであ
り第１図乃至第３図は経過日数と分光度との関係
曲線図、第４図はHI価と分光度との相関図であ
る。
Figures 1 to 4 show the performance of the stabilized peroxidase-labeled anti-human IgG (γ) of the present invention. is a correlation diagram between HI value and spectral intensity.
Claims (1)
緩衝液およびフエノールの混和液を添加したこと
を特徴とする安定化パーオキシダーゼ標識抗ヒト
IgG（γ）。 ２ 前記混和液にさらに牛血清アルブミンを添加
したことを特徴とする特許請求の範囲第１項記載
の安定化パーオキシダーゼ標識抗ヒトIgG（γ）。 ３ 緩衝液に、フエノール0.1％以下、又はフエ
ノール0.1％以下および牛血清アルブミン５％以
下を添加することを特徴とする特許請求の範囲第
１項記載の安定化パーオキシダーゼ標識抗ヒト
IgG（γ）。 ４ 緩衝液を、トリス（ヒドロキシメチル）アミ
ノメタン、ジエタノール、トリエタノール、リン
酸、酢酸の内から選定することを特徴とする特許
請求の範囲第１項記載の安定化パーオキシダーゼ
標識抗ヒトIgG（γ）。[Claims] 1. Peroxidase-labeled anti-human IgG (γ),
Stabilized peroxidase-labeled anti-human characterized by adding a mixture of buffer and phenol
IgG (γ). 2. The stabilized peroxidase-labeled anti-human IgG (γ) according to claim 1, wherein bovine serum albumin is further added to the mixed solution. 3. The stabilized peroxidase-labeled anti-human according to claim 1, characterized in that 0.1% or less of phenol, or 0.1% or less of phenol and 5% or less of bovine serum albumin are added to the buffer solution.
IgG (γ). 4. The stabilized peroxidase-labeled anti-human IgG ( γ).
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP4792484A JPS60192260A (en) | 1984-03-13 | 1984-03-13 | Stabilized peroxidase labeled antihuman igg(gamma) |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP4792484A JPS60192260A (en) | 1984-03-13 | 1984-03-13 | Stabilized peroxidase labeled antihuman igg(gamma) |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS60192260A JPS60192260A (en) | 1985-09-30 |
| JPH0531743B2 true JPH0531743B2 (en) | 1993-05-13 |
Family
ID=12788918
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP4792484A Granted JPS60192260A (en) | 1984-03-13 | 1984-03-13 | Stabilized peroxidase labeled antihuman igg(gamma) |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS60192260A (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0716736U (en) * | 1993-08-31 | 1995-03-20 | 岩谷産業株式会社 | Portable charcoal stove |
| JPH1019259A (en) * | 1996-06-27 | 1998-01-23 | Rutaka Kobayashi | Charcoal fire stove |
Families Citing this family (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS61205862A (en) * | 1985-03-08 | 1986-09-12 | Shionogi & Co Ltd | Reagent for measuring allergen specific igg antibody |
| DE3509238A1 (en) * | 1985-03-14 | 1986-09-18 | Boehringer Mannheim Gmbh, 6800 Mannheim | STABILIZATION OF PEROXIDASE ACTIVITY IN SOLUTION |
| JPS6463380A (en) * | 1987-09-03 | 1989-03-09 | Teijin Ltd | Stabilized peroxidase composition |
| CA2005511A1 (en) * | 1989-01-17 | 1990-07-17 | Harold C. Warren Iii | Enzyme-labeled receptor composition, diagnostic kit and use in method to determine a ligand |
| JPH03277297A (en) * | 1990-03-28 | 1991-12-09 | Saitetsuku Res:Kk | Determination of recombinant-type human angiotensinogen |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5446827A (en) * | 1977-09-19 | 1979-04-13 | Mamoru Sugiura | Measuring of immunoglobulin |
| JPS56102790A (en) * | 1980-01-07 | 1981-08-17 | Abbott Lab | Stabilization of peroxydizing enzyme in medium based on serum protein |
| JPS5925683A (en) * | 1982-08-03 | 1984-02-09 | Toyobo Co Ltd | Stable enzyme composition |
-
1984
- 1984-03-13 JP JP4792484A patent/JPS60192260A/en active Granted
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5446827A (en) * | 1977-09-19 | 1979-04-13 | Mamoru Sugiura | Measuring of immunoglobulin |
| JPS56102790A (en) * | 1980-01-07 | 1981-08-17 | Abbott Lab | Stabilization of peroxydizing enzyme in medium based on serum protein |
| JPS5925683A (en) * | 1982-08-03 | 1984-02-09 | Toyobo Co Ltd | Stable enzyme composition |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0716736U (en) * | 1993-08-31 | 1995-03-20 | 岩谷産業株式会社 | Portable charcoal stove |
| JPH1019259A (en) * | 1996-06-27 | 1998-01-23 | Rutaka Kobayashi | Charcoal fire stove |
Also Published As
| Publication number | Publication date |
|---|---|
| JPS60192260A (en) | 1985-09-30 |
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