CN111077323A - Insulin determination kit for eliminating insulin autoantibody interference - Google Patents
Insulin determination kit for eliminating insulin autoantibody interference Download PDFInfo
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- CN111077323A CN111077323A CN202010022770.1A CN202010022770A CN111077323A CN 111077323 A CN111077323 A CN 111077323A CN 202010022770 A CN202010022770 A CN 202010022770A CN 111077323 A CN111077323 A CN 111077323A
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- insulin
- autoantibody
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- eliminating
- determination
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- 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 title claims abstract description 169
- 229940125396 insulin Drugs 0.000 title claims abstract description 85
- 102000004877 Insulin Human genes 0.000 title claims abstract description 84
- 108090001061 Insulin Proteins 0.000 title claims abstract description 84
- 238000000034 method Methods 0.000 claims abstract description 13
- 239000003153 chemical reaction reagent Substances 0.000 claims description 10
- 239000003085 diluting agent Substances 0.000 claims description 7
- 210000002966 serum Anatomy 0.000 claims description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 4
- 230000002860 competitive effect Effects 0.000 claims description 3
- 239000007836 KH2PO4 Substances 0.000 claims description 2
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 claims description 2
- 229910000397 disodium phosphate Inorganic materials 0.000 claims description 2
- 229910000402 monopotassium phosphate Inorganic materials 0.000 claims description 2
- 239000011780 sodium chloride Substances 0.000 claims description 2
- 238000003149 assay kit Methods 0.000 claims 1
- 238000010790 dilution Methods 0.000 claims 1
- 239000012895 dilution Substances 0.000 claims 1
- 239000008363 phosphate buffer Substances 0.000 claims 1
- 238000003018 immunoassay Methods 0.000 abstract description 3
- 238000001514 detection method Methods 0.000 abstract 1
- 108010075254 C-Peptide Proteins 0.000 description 15
- VOUAQYXWVJDEQY-QENPJCQMSA-N 33017-11-7 Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)NCC(=O)NCC(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N1[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O)CCC1 VOUAQYXWVJDEQY-QENPJCQMSA-N 0.000 description 10
- 210000004153 islets of langerhan Anatomy 0.000 description 4
- 108010076181 Proinsulin Proteins 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 206010067584 Type 1 diabetes mellitus Diseases 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 210000000227 basophil cell of anterior lobe of hypophysis Anatomy 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 238000000691 measurement method Methods 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 208000034826 Genetic Predisposition to Disease Diseases 0.000 description 1
- 206010018429 Glucose tolerance impaired Diseases 0.000 description 1
- 102000008214 Glutamate decarboxylase Human genes 0.000 description 1
- 108091022930 Glutamate decarboxylase Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 206010022489 Insulin Resistance Diseases 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 102000004248 Zinc Transporter 8 Human genes 0.000 description 1
- 108090000702 Zinc Transporter 8 Proteins 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 230000036046 immunoreaction Effects 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 238000011545 laboratory measurement Methods 0.000 description 1
- 239000006249 magnetic particle Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 208000001072 type 2 diabetes mellitus Diseases 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 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
- G01N33/74—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving hormones or other non-cytokine intercellular protein regulatory factors such as growth factors, including receptors to hormones and growth factors
-
- 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
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
- G01N2333/575—Hormones
- G01N2333/62—Insulins
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/04—Endocrine or metabolic disorders
- G01N2800/042—Disorders of carbohydrate metabolism, e.g. diabetes, glucose metabolism
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Chemical & Material Sciences (AREA)
- Biomedical Technology (AREA)
- Urology & Nephrology (AREA)
- Hematology (AREA)
- Microbiology (AREA)
- Cell Biology (AREA)
- Biotechnology (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)
- Endocrinology (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention discloses an insulin determination kit for eliminating insulin autoantibody interference, and belongs to the technical field of immunoassay. The technical scheme of the invention is as follows: the method is not influenced by the insulin autoantibody when detecting the insulin, and the using method is the same as the original chemiluminescence method, so that the method is economical, convenient and easy to implement and is an insulin detection method with higher accuracy.
Description
Technical Field
The invention belongs to the technical field of immunoassay; or a method of testing a material by measuring a color change resulting from a reaction using visible light.
Background
Normally, insulin is mainly secreted and released into blood from human islet cells, during a series of processes for producing insulin, the islet cells first synthesize proinsulin, which is a long protein chain, and the proinsulin is decomposed into three segments under the action of enzyme, the front and rear segments are reconnected to form insulin consisting of an A chain and a B chain, and the middle segment is separated and called C peptide.
In the β cell secretion of the pancreatic islet, the total gram molecular weight of the insulin and the C peptide is equal, in the clinical laboratory measurement, the common unit of the insulin is uIU/ml, the unit of the C peptide is ng/ml, the half-life of the insulin is 4.8min, and the C peptide is 11 min proinsulin is 17.5 min.
Type 1 diabetes mellitus is caused by the destruction of β cells mediated by T cells and has a genetic predisposition, characterized by the presence in the serum of patients of circulating autoantibodies including Islet Cell Antibodies (ICA), glutamate decarboxylase antibodies (GADA), tyrosine phosphatase antibodies (IA-2A), insulin antibodies (IAA) and zinc transporter 8 antibodies (ZnT8A), IAA, an insulin autoantibody, which is 20-30% positive in pre-diabetic and type 1 diabetes mellitus diabetic patients treated with xenogenic insulin, the serum of which often has an anti-insulin anti-antibody (IAB) present, which binds to insulin to form a complex, inactivating insulin, one of the major causes of insulin resistance.
The invention content is as follows:
in order to solve the problem that the determination of serum insulin is interfered by an endogenous insulin autoantibody in the prior art, the invention provides the chemiluminescence determination method which is economic, convenient and easy to implement, has higher accuracy and can eliminate the influence of the endogenous insulin autoantibody.
The technical scheme is as follows: when the serum is added into the sample diluent, the insulin autoantibody secondary antibody and the insulin autoantibody generate antigen-antibody reaction, so that competitive reaction between the insulin autoantibody and the insulin antibody and insulin in the determination reagent is sealed, and the occurrence of reaction interference in insulin determination is avoided.
The specific implementation mode is as follows:
the present invention is further illustrated by the following example of serum insulin measurement using the Ampere A2000PLUS chemiluminescence analyzer.
Example 1
The composition of the reagent is as follows:
a. the insulin reagent is a reagent matched with Zhengzhou Antu bioengineering GmbH, adopts a double-antigen sandwich method principle to detect, uses insulin antibody to coat magnetic particles, uses horseradish peroxidase to mark the insulin antibody to prepare an enzyme conjugate, forms an antibody-antigen-antibody-enzyme labeled compound through immunoreaction, and the compound catalyzes a luminescent substrate to emit photons, wherein the luminescent intensity is in direct proportion to the content of insulin.
b. The sample diluent is the diluent prepared by the invention: 0.15M KH2PO40.2 g, Na2HPO4·12H2O2.9 g, NaCl 8.0 g, KCl 0.2 g, Tween-200.5 ml distilled water to 1000ml, and insulin autoantibody secondary antibody with 20IU/ml concentration.
c. The insulin autoantibody determination kit (chemiluminescence method) is produced by Shenzhen Yahulong Biotech limited.
Example 2
The composition of the reagent is as follows:
a. the insulin reagent is a matching reagent of Zhengzhou Antu bioengineering GmbH.
b. The sample diluent is a reagent matched with Zhengzhou Antu bioengineering GmbH.
c. The insulin autoantibody determination kit (chemiluminescence method) is produced by Shenzhen Yahulong Biotech limited.
Example 3
1. Detecting an object: 128 hospital examiners, of which there are 60 insulin autoantibody positives, 32 males, with a mean age of 48.5 years; 28 women, mean age 46.5 years; of these, 64 insulin autoantibody negative cases, male, 34 cases, mean age 49.5 years; 30 women, average age 48.5 years old.
2. The method comprises the following steps: 128 subjects were tested for insulin, C-peptide, and insulin autoantibodies in example 1 and example 2, respectively, and the insulin and C-peptide changes in the insulin autoantibody positive group and the insulin autoantibody negative group were compared.
3. The instrument comprises the following steps: an AutoLumo A2000PLUS chemiluminescence detector, and an iFlash 3000 chemiluminescence immunoassay analyzer.
4. Results
4.1 insulin, C-peptide, of the insulin autoantibody negative group was determined using examples 1 and 2, comparing as shown in Table 1:
TABLE 1. example 1 and example assay 2 determination of insulin autoantibody (COI) negative group insulin (uIU/ml), C peptide (ng/ml) comparison
4.2 insulin, C-peptide, positive groups of insulin autoantibodies were determined using examples 1 and 2, comparing as shown in Table 2:
TABLE 2 comparison of insulin (uIU/ml) and C-peptide (ng/ml) in insulin autoantibody (COI) positive groups determined in example 1 and example assay 2
| Project number IAA insulin C peptide insulin/C peptide |
| Example 16055.6. + -. 38.712.47. + -. 9.983.14. + -. 2.463.97 |
| Example 26055.6. + -. 38.73.06. + -. 3.663.16. + -. 2.420.97 |
As can be seen from the above experiments, in the negative group for measuring insulin autoantibodies, there was no significant difference in the insulin measurement values of the measurement methods of the present invention in example 1 and example 2, t =1.01,P=0.6224, n =64, insulin/C-peptide ratio of around 4.0, insulin levels higher than C-peptide levels; in the positive group for determination of insulin autoantibodiesThe insulin measurement values of the measurement methods of the present invention in example 1 and example 2 were highly significantly different from each other, t =64.39,P=0.0051, n =60, insulin/C-peptide is 1.0 or less, and insulin levels are lower than C-peptide levels. The method of the invention can ensure the accuracy of the insulin determination result by adding the insulin autoantibody secondary antibody.
The comparison shows that the insulin autoantibody is sealed by the insulin autoantibody secondary antibody, so that the competitive reaction of the insulin autoantibody and the insulin antibody and insulin in the determination reagent is eliminated, the occurrence of the interference of the insulin determination reaction is avoided, and the method has popularization and application prospects.
Claims (3)
1. The invention discloses an insulin determination kit for eliminating insulin autoantibody interference, which is characterized in that a sample diluent contains an insulin autoantibody secondary antibody, the insulin autoantibody secondary antibody in the sample diluent is combined with an insulin autoantibody in serum, and competitive reaction between the insulin autoantibody and the insulin antibody and insulin in an insulin determination reagent is eliminated.
2. The kit for measuring insulin for eliminating interference of insulin autoantibody according to claim 1, wherein the dilution of the sample by the chemiluminescence method comprises per liter: 0.15M KH2PO40.2 g, Na2HPO4·12H2O2.9 g, NaCl 8.0 g, KCl 0.2 g, Tween-200.5 ml, and the concentration of the insulin autoantibody secondary antibody is 10000-30000 IU.
3. The insulin assay kit for eliminating interference of insulin autoantibodies according to claim 1, wherein the concentration of phosphate buffer in the sample diluent is 150mmol/L and the pH value is 7.2 ± 0.2.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202010022770.1A CN111077323A (en) | 2020-01-12 | 2020-01-12 | Insulin determination kit for eliminating insulin autoantibody interference |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202010022770.1A CN111077323A (en) | 2020-01-12 | 2020-01-12 | Insulin determination kit for eliminating insulin autoantibody interference |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN111077323A true CN111077323A (en) | 2020-04-28 |
Family
ID=70322659
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202010022770.1A Pending CN111077323A (en) | 2020-01-12 | 2020-01-12 | Insulin determination kit for eliminating insulin autoantibody interference |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN111077323A (en) |
Citations (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5804391A (en) * | 1994-11-04 | 1998-09-08 | Boehringer Mannheim Gmbh | Elimination of rheumatoid factor interference using anti-FD antibodies |
| US6632682B1 (en) * | 1987-05-23 | 2003-10-14 | Dade Behring Marburg Gmbh | One-step immunoassay for the determination of antigen-specific antibodies of one of the immunoglobulin classes A, M, D, or E, and an agent suitable for this purpose |
| CN1888904A (en) * | 2005-06-27 | 2007-01-03 | 上海透景生命科技有限公司 | Method for indicating xenotropic antibody interference in immune reaction |
| US20090176252A1 (en) * | 2005-06-29 | 2009-07-09 | Shibayagi Co., Ltd. | Method for the Measurement of Endocrine Substances In an Analyte |
| US20090246800A1 (en) * | 2006-10-26 | 2009-10-01 | Abbott Laboratories | Immunoassay of analytes in samples containing endogenous anti-analyte antibodies |
| US20110136103A1 (en) * | 2009-12-03 | 2011-06-09 | Abbott Laboratories | Autoantibody enhanced immunoassays and kits |
| US20110136141A1 (en) * | 2009-12-03 | 2011-06-09 | Abbott Laboratories | Peptide reagents and method for inhibiting autoantibody antigen binding |
| CN203385722U (en) * | 2013-10-11 | 2014-01-08 | 重庆奥创生物技术开发有限责任公司 | IgM (Immunoglobulin M) detection test strip capable of eliminating IgG (Immunoglobulin G) interference |
| CN107286239A (en) * | 2016-03-30 | 2017-10-24 | 复旦大学 | Compound of antibody with autoantibody or similar anti self antibody and preparation method thereof |
| CN109239329A (en) * | 2018-10-18 | 2019-01-18 | 郑州安图生物工程股份有限公司 | A kind of insulin immue quantitative detection reagent box |
-
2020
- 2020-01-12 CN CN202010022770.1A patent/CN111077323A/en active Pending
Patent Citations (10)
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|---|---|---|---|---|
| US6632682B1 (en) * | 1987-05-23 | 2003-10-14 | Dade Behring Marburg Gmbh | One-step immunoassay for the determination of antigen-specific antibodies of one of the immunoglobulin classes A, M, D, or E, and an agent suitable for this purpose |
| US5804391A (en) * | 1994-11-04 | 1998-09-08 | Boehringer Mannheim Gmbh | Elimination of rheumatoid factor interference using anti-FD antibodies |
| CN1888904A (en) * | 2005-06-27 | 2007-01-03 | 上海透景生命科技有限公司 | Method for indicating xenotropic antibody interference in immune reaction |
| US20090176252A1 (en) * | 2005-06-29 | 2009-07-09 | Shibayagi Co., Ltd. | Method for the Measurement of Endocrine Substances In an Analyte |
| US20090246800A1 (en) * | 2006-10-26 | 2009-10-01 | Abbott Laboratories | Immunoassay of analytes in samples containing endogenous anti-analyte antibodies |
| US20110136103A1 (en) * | 2009-12-03 | 2011-06-09 | Abbott Laboratories | Autoantibody enhanced immunoassays and kits |
| US20110136141A1 (en) * | 2009-12-03 | 2011-06-09 | Abbott Laboratories | Peptide reagents and method for inhibiting autoantibody antigen binding |
| CN203385722U (en) * | 2013-10-11 | 2014-01-08 | 重庆奥创生物技术开发有限责任公司 | IgM (Immunoglobulin M) detection test strip capable of eliminating IgG (Immunoglobulin G) interference |
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|---|
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