CN102565420B - Human serum glycated albumin array kit - Google Patents
Human serum glycated albumin array kit Download PDFInfo
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- CN102565420B CN102565420B CN2011104408656A CN201110440865A CN102565420B CN 102565420 B CN102565420 B CN 102565420B CN 2011104408656 A CN2011104408656 A CN 2011104408656A CN 201110440865 A CN201110440865 A CN 201110440865A CN 102565420 B CN102565420 B CN 102565420B
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Abstract
The invention provides a human serum glycated albumin assay kit which comprises a reagent 1 and a reagent 2, wherein the reagent 1 comprises the following components: 20-200mmol/L of buffer solution, 5-50KU/L of protease co-expression vector, 10-50KU/L of peroxisome, 2-20mmol/L of 4-amino antipyrine, 0.01-1% of preservative and 0.01-1% of stabilizer, and the protease co-expression vector is obtained by cloning a protease gene and an ascorbic acid oxidase gene onto a same vector for performing co-expression; and the reagent 2 comprises the following components: 20-200mmol/L of buffer solution, 5-50U/mL of fructose lysine enzyme, 1-10mmol/L of N, N-bis(4-sulfobutyl ether)-3-methylaniline, 0.01-1% of preservative and 0.01-1% of stabilizer. The kit can remove the interferences of globulin and ascorbic acid in human serum and has good stability and low cost.
Description
Technical field
The present invention relates to the medical test technical field, be specifically related to a kind of human serum glycated albumin array kit.
Background technology
Diabetes are to act on that body causes hypoinsulinism, insulin resistant etc. and a series of metabolism disorder syndromes such as the sugar that causes, protein, fat, power and water Xie Zhi by various virulence factors such as inherited genetic factors, immunologic function disorder, infected by microbes and toxin thereof, free radical toxin, mental elements, are one of several large diseases of harm humans disease.
In human serum, albumin accounts for 66% of serum protein, and all the other are immunoglobulin (Ig); The glycosylation of non-enzymatic occurs in the N-end of glucose in serum and serum protein, generates glycated serum protein, and glycosylated albumin accounts for more than 90% of glycated serum protein.In addition, because albumin stable content in serum exists, sphaeroprotein can be because the disease factors such as infection cause fluctuation; Therefore the Accurate Determining glycosylated albumin to the accurate response diabetes the glycemic control situation extremely important.
So the glycosylated albumin amount in human serum of how accurately determining becomes the key of clinical detection glycosylated albumin.Existing market mainly adopts enzyme process for detection of the glycosylated albumin in human serum, its reaction principle, at first using proteolytic enzyme that glycated protein is digested to low-molecular-weight saccharification polypeptide, is used fructosyl amino acid enzyme catalysis saccharification polypeptide generation oxidizing reaction to generate polypeptide (or amino acid), arabino-hexosone and H subsequently
2O
2, the H of release
2O
2By the end reaction colorimetry, measure, the concentration of its absorption value at the 600nm place and glycosylated albumin is proportional.Concrete reaction process is as follows:
And there is following defect in enzyme process glycosylated albumin in the market:
(1) can not get rid of the interference of sphaeroprotein fully: the protease substrate poor specificity adopted, to all albumen kinds in serum, can be decomposed, therefore can't get rid of the interference of sphaeroprotein;
(2) test kit poor stability: because coupling is the Trinder reaction, and this reaction is vulnerable to the interference of reducing substances, owing to inputting in a large number at present the causes of the reducing substanceses such as xitix, in a lot of patients serums, high reducing substance causes very large interference to reaction; And the Vitamin C oxidase that the removal xitix adopts easily is subject to the decomposition of proteolytic enzyme; Self-decomposition reaction, poor stability also can occur in proteolytic enzyme self;
(3) the test kit cost is high: for glycosylated albumin is decomposed into to glycated amino acid fully, in order to participate in the next step, therefore adopt the proteolytic enzyme of high density, the enzyme amount adopted is also very high, therefore cause the test kit holistic cost very high;
(4) existing glycosylated albumin does not provide term of reference in the market, only provides glycosylated albumin/albuminous term of reference, for clinical guidance, certain defect is arranged.
Summary of the invention
Technical problem to be solved by this invention is to provide a kind of human serum glycated albumin array kit, and it is low that this test kit can be got rid of in human serum interference, good stability, the cost of sphaeroprotein and xitix.
The technical solution adopted in the present invention is:
A kind of human serum glycated albumin array kit, this test kit comprises reagent 1 and reagent 2, wherein:
Reagent 1:
Reagent 2:
Wherein, described proteolytic enzyme coexpression body refers to the gene clone of the gene of proteolytic enzyme and Vitamin C oxidase on identical carrier, then this carrier is transformed to Host Strains, realize the coexpression of micromolecular proteolytic enzyme and macromolecular Vitamin C oxidase in same Host Strains, and the protein that contains proteolytic enzyme, these two kinds of enzymes of Vitamin C oxidase obtained.
The gene of described proteolytic enzyme can be the gene that includes the proteinase gene sequence in arbitrary source, be preferably the gene that Aspergillus or bacillus or wheat axle obstruct mould genus source, the gene in the woods Bai Shi Candida albicans that more preferably enzyme activity is high (Tritirachium album libmer) source, the proteolytic enzyme obtained is Proteinase K (Proteinase K).Can find the complete genome sequence of this enzyme from the GENBANK of NCBI.
The gene of described Vitamin C oxidase can be the gene that includes the Vitamin C oxidase gene order in arbitrary source, is preferably the gene of plant origin, more preferably the gene in cucumber (Cucumis sp.) source.Can find the complete genome sequence of this enzyme from the GENBANK of NCBI.
Expression system can adopt protokaryon or eukaryotic expression system, as long as it can realize correction, and preferred prokaryotic expression system, because the background of prokaryotic expression system is comparatively simple, and the cycle is shorter.
The proteolytic enzyme that described proteolytic enzyme coexpression body gives expression to and the N of Vitamin C oxidase end all have the increase of 5-30 amino acid fragment, all add the nucleotide sequence (a corresponding 5-30 amino acid) of 15-90bp in molecular cloning at the 5 ' end of both sequences, these amino acid whose major functions are:
1, facilitate the connection of two kinds of enzymes, comprise restriction enzyme site etc.;
2, guarantee the formation of two kinds of correct conformations of enzyme, thereby guarantee the vigor of two kinds of enzymes;
3, the Enhancin enzyme is for albuminous specificity;
4, avoid the oxidasic Decomposition of proteolytic enzyme Ascorbic Acid;
5, add suitable label, be convenient to the separation and purification in later stage.
Described damping fluid is a kind of in Tri(Hydroxymethyl) Amino Methane Hydrochloride damping fluid, acetic acid-sodium acetate buffer, phthalic acid-hydrochloride buffer or glycine-hydrochloride buffer.
Described sanitas is a kind of in MIT or proclin300.
Described stablizer is a kind of in glycerine, bovine serum albumin (BSA), tween 20.
Micromolecular proteolytic enzyme and macromolecular Vitamin C oxidase coexpression technological line are as follows:
1, obtain the full length gene fragment of proteolytic enzyme and ascorbase;
2, the nucleotide sequence that proteolytic enzyme and 5 ' end of xitix gene fragment is added to a corresponding 5-30 amino acid fragment;
3, be connected into identical carrier by two kinds, proceed to and express in bacterium;
4, clonal expression, protein separation;
5, determination of activity, measure respectively that enzyme is lived, proteolytic enzyme is for the stability of albuminous specificity, coexpression thing:
(1) proteolytic enzyme measuring method for activity, any measuring method for activity gets final product, as long as guarantee that measuring method for activity is consistent.As: 37 ℃, it is 1 enzyme unit alive that 1min produces the needed enzyme amount of 1 μ mol tyrosine; The 3mL reaction system, containing the 42mM potassium phosphate buffer, 0.5% milk casein, 1.5mM sodium-acetate, the proteolytic enzyme of 0.1-0.2U; Wherein, adopt tyrosine Criterion curve.
(2) specificity of proteolytic enzyme coexpression body: the milk casein in above-mentioned (1) measuring method for activity is replaced with to sphaeroprotein, found that, the proteolytic enzyme that no matter adds many high densitys, all, without colour developing, illustrate that the proteolytic enzyme coexpression body screened is high to the albumin specificity in human serum.
(3) Vitamin C oxidase measuring method for activity: any measuring method for activity gets final product, as long as guarantee that measuring method for activity is consistent.As: 37 ℃, it is 1 enzyme unit alive that 1min reduces the needed enzyme amount of 1mmol xitix; The 3mL reaction system, containing 80mM potassium primary phosphate, 10mM Sodium phosphate dibasic, 0.5mM xitix, 1mM EDTA, 1g/LBSA and 0.1-0.2U/mL enzyme liquid; Wherein, adopt xitix Criterion curve.
(4) stability of proteolytic enzyme coexpression body: proteolytic enzyme coexpression body is positioned over to 4 ℃, every 1 month, adopt the standard measuring method for activity to measure the once vigor of two kinds of enzymes, find that 4 ℃ of preservation vigor half a year only have 10% decline, illustrate that the proteolytic enzyme coexpression body stability be sieved to is very high, be applicable to the preparation of glycosylated albumin test kit fully.
Human serum glycated albumin array kit of the present invention, except comprising reagent 1 and reagent 2, also comprises calibration object, and calibration object is the solution containing albumin and glycosylated albumin.The preparation process of calibration object is: human serum albumin is mixed with weight ratio (w/w) with glucose in 1: 1～1: 100, hatch ten days for 37 ℃, glucose is removed in dialysis, by Reagent kit of glucose, measure without after glucose, employing HPLC measures the content of glycosylated albumin and accounts for the ratio of total protein, and be 200-1000 μ M by this solution dilution, lyophilize, as calibration object, adopts HPLC to carry out definite value to calibration object.
According to calibration object and reagent 1, reagent 2, select the individual serum of 120 parts of health examinations, the term of reference of measuring glycosylated albumin is 100～285 μ mol/L, measure albumin simultaneously, updating formula is glycosylated albumin/albumin=(glycosylated albumin concentration * 0.23+1.12)/albumin concentration, show that glycosylated albumin/albuminous term of reference is 11～16%.After formula correction, the present invention provides glycosylated albumin/albuminous ratio.Provide glycosylated albumin and glycosylated albumin/albuminous term of reference more favourable to clinical monitoring diabetes after this correction.
The present invention adopts advanced modern molecular biology technique, by micromolecular proteolytic enzyme and macromolecular Vitamin C oxidase coexpression, has done so following advantage:
1, two kinds of independent vigor of enzyme remain unchanged;
2, proteolytic enzyme strengthens for albuminous specificity, and the reaction vigor of sphaeroprotein is descended, thereby has avoided to a certain extent the interference of sphaeroprotein;
3, proteolytic enzyme can't act on Vitamin C oxidase, therefore latter's stability improves, test kit stability improves;
4, the proteolytic enzyme adopted and Vitamin C oxidase amount all reduce, the test kit cost;
5, owing to adopting clonal expression, can great expression, produce the enzyme cost.
Embodiment
Below in conjunction with embodiment, the present invention is further described in detail, but is not limited to this.
A kind of human serum glycated albumin array kit, comprise reagent 1 and reagent 2, wherein:
Reagent 1:
Reagent 2:
Proteinase K coexpression system is standby:
1. the full gene of proteolytic enzyme coexpression body is synthetic: find woods Bai Shi Candida albicans (Tritirachium album limber) Proteinase K gene order from GENBANK, add 30bp Nucleotide at its gene order 5 ' end, comprise and add restriction enzyme site NdeI, 3 ' end is removed its termination codon, cucumber source (Cucumis sp.) Vitamin C oxidase gene order 5 ' end adds 120bp Nucleotide, same its termination codon of removing of 3 ' end, add restriction enzyme site XhoI, two terminal sequences are combined that to carry out full gene synthetic;
2. recombination is connected in the simple and easy carrier of cloning vector pMD-18-T;
3. be connected in expression vector pET22b;
4. proceed to and express in bacterium ROSEETA;
5. 37 ℃ of long bacterium, add IPTG=0.1mM to induce and produce enzyme coexpression body during OD=0.6-0.8;
6. adopt the nickel affinity column to carry out purifying.
The preparation of the present embodiment glycosylated albumin standard substance and definite value: human serum albumin (50g/L) mixes with the glucose saturated solution, add the 1g/L sodium azide to cook sanitas, hatch ten days for 37 ℃, adopt normal saline dialysis to remove glucose, measure and determine not containing glucose by Reagent kit of glucose, employing HPLC measures the content of glycosylated albumin and accounts for the ratio of total protein, and is that concentration is 500 μ M by this solution dilution, and lyophilize is as calibration object.
The raw material that embodiment is used, unless otherwise indicated, be commercially available industrial goods.
The above embodiment of the present invention is to explanation of the present invention and can not be for limiting the present invention, and the implication suitable with claims of the present invention and any change in scope, all should think to be included in the scope of claims.
Claims (7)
1. a human serum glycated albumin array kit is characterized in that: comprise reagent 1 and reagent 2, wherein:
Reagent 1:
Reagent 2:
Wherein, described proteolytic enzyme coexpression body refers to the gene clone of the gene of proteolytic enzyme and Vitamin C oxidase realize the protein that coexpression obtains in same Host Strains on identical carrier; Described damping fluid is a kind of in Tri(Hydroxymethyl) Amino Methane Hydrochloride damping fluid, acetic acid-sodium acetate buffer, phthalic acid-hydrochloride buffer or glycine-hydrochloride buffer; Described sanitas is a kind of in MIT or proclin300; Described stablizer is a kind of in glycerine, bovine serum albumin, tween 20.
2. human serum glycated albumin array kit according to claim 1 is characterized in that: the gene of described proteolytic enzyme is the gene that Aspergillus or bacillus or wheat axle obstruct mould genus source.
3. human serum glycated albumin array kit according to claim 2, is characterized in that: the gene that the gene of described proteolytic enzyme is woods Bai Shi Candida albicans source.
4. human serum glycated albumin array kit according to claim 1, is characterized in that: the gene that the gene of described Vitamin C oxidase is plant origin.
5. human serum glycated albumin array kit according to claim 4, is characterized in that: the gene that the gene of described Vitamin C oxidase is the cucumber source.
6. human serum glycated albumin array kit according to claim 1 is characterized in that: the proteolytic enzyme that described proteolytic enzyme coexpression body gives expression to and the N of Vitamin C oxidase end all have the increase of 5-30 amino acid fragment.
7. human serum glycated albumin array kit according to claim 1, it is characterized in that: also comprise calibration object, calibration object is the solution containing albumin and glycosylated albumin, the preparation process of calibration object is: human serum albumin is mixed with weight ratio 1:1～1:100 with glucose, hatch ten days for 37 ℃, glucose is removed in dialysis, by Reagent kit of glucose, measure without after glucose, employing HPLC measures the content of glycosylated albumin and accounts for the ratio of total protein, and be 200-1000 μ M by this solution dilution, lyophilize is as calibration object, adopt HPLC to carry out definite value to calibration object, according to calibration object and reagent 1, reagent 2, select the individual serum of 120 parts of health examinations, the term of reference of measuring glycosylated albumin is 100～285 μ mol/L, measure albumin simultaneously, updating formula is glycosylated albumin/albumin=(glycosylated albumin concentration * 0.23+1.12)/albumin concentration, show that glycosylated albumin/albuminous term of reference is 11～16%.
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Families Citing this family (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN104345150A (en) * | 2013-07-26 | 2015-02-11 | 深圳市艾瑞生物科技有限公司 | Glycated albumin detection immunochromatography test trip and preparation method thereof |
| CN104198472B (en) * | 2014-08-14 | 2017-11-10 | 上海睿康生物科技有限公司 | A kind of glycosylated albumin detection kit of stabilization |
| CN104673878B (en) * | 2015-03-13 | 2017-01-11 | 温州医科大学 | Kit for measuring concentration ratio of glycated albumin and albumin by virtue of single system |
| CN105092336A (en) * | 2015-08-28 | 2015-11-25 | 宁波瑞源生物科技有限公司 | Preparation method of stable glycated albumin calibrating material and quality control material |
| CN107525774A (en) * | 2016-06-21 | 2017-12-29 | 山东博科生物产业有限公司 | Potassium hydroxide method total protein diagnostic test kits |
| CN108070634B (en) * | 2017-11-24 | 2021-04-06 | 宁波美康保生生物医学工程有限公司 | Three-item combined detection reagent tray for diabetes |
| CN109839297B (en) * | 2018-07-31 | 2021-06-08 | 深圳市安帝宝科技有限公司 | Method for rapidly preparing glycated albumin standard substance |
| CN109991426A (en) * | 2019-04-03 | 2019-07-09 | 深圳市安帝宝科技有限公司 | A kind of glycated albumin detection kit |
Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2007107950A (en) * | 2005-10-12 | 2007-04-26 | Bml Inc | Control sample of glycated albumin |
| JP2007163515A (en) * | 2002-06-18 | 2007-06-28 | Asahi Kasei Pharma Kk | Measuring substance for glycated protein measurement, and standard measurement method |
| CN101023168A (en) * | 2004-08-05 | 2007-08-22 | 旭化成制药株式会社 | Reagent containing protease reaction promoter and/or colorant stabilizer |
| CN101297044A (en) * | 2005-10-27 | 2008-10-29 | 爱科来株式会社 | Albumin-denaturing agent |
| CN101493467A (en) * | 2008-01-25 | 2009-07-29 | 上海伊思柏生物科技有限公司 | Quantitative determination method for saccharified protein |
| CN201689054U (en) * | 2010-05-27 | 2010-12-29 | 上海执诚生物技术有限公司 | Kit for detecting glycated albumin content in blood |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2001090735A1 (en) * | 2000-05-23 | 2001-11-29 | Koji Sode | Kit for assaying saccharified protein |
| JP4985214B2 (en) * | 2007-08-20 | 2012-07-25 | ソニー株式会社 | Biological substance detection method using laser |
-
2011
- 2011-12-26 CN CN2011104408656A patent/CN102565420B/en active Active
Patent Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2007163515A (en) * | 2002-06-18 | 2007-06-28 | Asahi Kasei Pharma Kk | Measuring substance for glycated protein measurement, and standard measurement method |
| CN101023168A (en) * | 2004-08-05 | 2007-08-22 | 旭化成制药株式会社 | Reagent containing protease reaction promoter and/or colorant stabilizer |
| JP2007107950A (en) * | 2005-10-12 | 2007-04-26 | Bml Inc | Control sample of glycated albumin |
| CN101297044A (en) * | 2005-10-27 | 2008-10-29 | 爱科来株式会社 | Albumin-denaturing agent |
| CN101493467A (en) * | 2008-01-25 | 2009-07-29 | 上海伊思柏生物科技有限公司 | Quantitative determination method for saccharified protein |
| CN201689054U (en) * | 2010-05-27 | 2010-12-29 | 上海执诚生物技术有限公司 | Kit for detecting glycated albumin content in blood |
Non-Patent Citations (8)
| Title |
|---|
| David A Rubenstein et al.Original investigation and glycated serum albumin on endothelial cells and platelets.《 Cardiovascular Diabetology 》.2010,第9卷(第28期),全文. |
| Masafumi Koga et al.Serum glycated albumin levels, but not glycated hemoglobin, is low in relation to glycemia in non-diabetic men with nonalcoholic fatty liver disease with high alanine aminotransferase levels.《Clinical Biochemistry》.2010,第43卷(第12期),1023-1025. |
| Original investigation and glycated serum albumin on endothelial cells and platelets;David A Rubenstein et al;《 Cardiovascular Diabetology 》;20100706;第9卷(第28期);全文 * |
| Serum glycated albumin levels, but not glycated hemoglobin, is low in relation to glycemia in non-diabetic men with nonalcoholic fatty liver disease with high alanine aminotransferase levels;Masafumi Koga et al;《Clinical Biochemistry》;20100831;第43卷(第12期);1023-1025 * |
| 沈霞等.酶法测定糖化白蛋白及其临床意义.《检验医学》.2006,第21卷(第2期),132-135. |
| 贾珂珂等.酮胺氧化酶法测定糖化白蛋白的评价.《中国实验诊断学》.2010,第14卷(第10期),1620-1623. |
| 酮胺氧化酶法测定糖化白蛋白的评价;贾珂珂等;《中国实验诊断学》;20101031;第14卷(第10期);1620-1623 * |
| 酶法测定糖化白蛋白及其临床意义;沈霞等;《检验医学》;20061231;第21卷(第2期);132-135 * |
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