CN1778937A - Determination of blood ammonia content and blood ammonia diagnostic reagent kit - Google Patents
Determination of blood ammonia content and blood ammonia diagnostic reagent kit Download PDFInfo
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- CN1778937A CN1778937A CN 200410065557 CN200410065557A CN1778937A CN 1778937 A CN1778937 A CN 1778937A CN 200410065557 CN200410065557 CN 200410065557 CN 200410065557 A CN200410065557 A CN 200410065557A CN 1778937 A CN1778937 A CN 1778937A
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- blood ammonia
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- nadph
- damping fluid
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- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 title claims abstract description 111
- 239000003153 chemical reaction reagent Substances 0.000 title claims abstract description 58
- 229910021529 ammonia Inorganic materials 0.000 title claims abstract description 55
- 239000008280 blood Substances 0.000 title claims abstract description 44
- 210000004369 blood Anatomy 0.000 title claims abstract description 44
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 claims abstract description 55
- 239000005515 coenzyme Substances 0.000 claims abstract description 36
- 238000000034 method Methods 0.000 claims abstract description 33
- ZKHQWZAMYRWXGA-KQYNXXCUSA-J ATP(4-) Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O ZKHQWZAMYRWXGA-KQYNXXCUSA-J 0.000 claims abstract description 21
- ZKHQWZAMYRWXGA-UHFFFAOYSA-N Adenosine triphosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)C(O)C1O ZKHQWZAMYRWXGA-UHFFFAOYSA-N 0.000 claims abstract description 21
- 102000005396 glutamine synthetase Human genes 0.000 claims abstract description 18
- 108020002326 glutamine synthetase Proteins 0.000 claims abstract description 18
- 238000013016 damping Methods 0.000 claims description 27
- 239000012530 fluid Substances 0.000 claims description 27
- 229960002989 glutamic acid Drugs 0.000 claims description 27
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 claims description 27
- 238000006243 chemical reaction Methods 0.000 claims description 26
- XJLXINKUBYWONI-DQQFMEOOSA-N [[(2r,3r,4r,5r)-5-(6-aminopurin-9-yl)-3-hydroxy-4-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(2s,3r,4s,5s)-5-(3-carbamoylpyridin-1-ium-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate Chemical compound NC(=O)C1=CC=C[N+]([C@@H]2[C@H]([C@@H](O)[C@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](OP(O)(O)=O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 XJLXINKUBYWONI-DQQFMEOOSA-N 0.000 claims description 25
- 108020000311 Glutamate Synthase Proteins 0.000 claims description 23
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims description 22
- -1 2-oxoglutaric acid ester Chemical class 0.000 claims description 20
- 239000000872 buffer Substances 0.000 claims description 13
- 230000001186 cumulative effect Effects 0.000 claims description 13
- 239000003795 chemical substances by application Substances 0.000 claims description 12
- 238000009007 Diagnostic Kit Methods 0.000 claims description 11
- 239000000203 mixture Substances 0.000 claims description 10
- 230000035484 reaction time Effects 0.000 claims description 8
- 239000002126 C01EB10 - Adenosine Substances 0.000 claims description 6
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 claims description 6
- 229910019142 PO4 Inorganic materials 0.000 claims description 6
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 claims description 6
- 230000007423 decrease Effects 0.000 claims description 6
- 239000001177 diphosphate Substances 0.000 claims description 6
- XPPKVPWEQAFLFU-UHFFFAOYSA-J diphosphate(4-) Chemical compound [O-]P([O-])(=O)OP([O-])([O-])=O XPPKVPWEQAFLFU-UHFFFAOYSA-J 0.000 claims description 6
- 235000011180 diphosphates Nutrition 0.000 claims description 6
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 claims description 6
- 239000010452 phosphate Substances 0.000 claims description 6
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 claims description 4
- DFPAKSUCGFBDDF-UHFFFAOYSA-N Nicotinamide Chemical compound NC(=O)C1=CC=CN=C1 DFPAKSUCGFBDDF-UHFFFAOYSA-N 0.000 claims description 4
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 claims description 3
- 239000002953 phosphate buffered saline Substances 0.000 claims description 3
- 229960004418 trolamine Drugs 0.000 claims description 3
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 claims description 2
- 150000004676 glycans Chemical class 0.000 claims description 2
- 235000011187 glycerol Nutrition 0.000 claims description 2
- 229960003966 nicotinamide Drugs 0.000 claims description 2
- 235000005152 nicotinamide Nutrition 0.000 claims description 2
- 239000011570 nicotinamide Substances 0.000 claims description 2
- BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 claims description 2
- 150000003839 salts Chemical class 0.000 claims description 2
- 150000005846 sugar alcohols Polymers 0.000 claims description 2
- YMAWOPBAYDPSLA-UHFFFAOYSA-N glycylglycine Chemical compound [NH3+]CC(=O)NCC([O-])=O YMAWOPBAYDPSLA-UHFFFAOYSA-N 0.000 claims 2
- 229940058020 2-amino-2-methyl-1-propanol Drugs 0.000 claims 1
- PDLNHDSYGLTYDS-UHFFFAOYSA-N 3-aminopropanoic acid;hydrochloride Chemical compound Cl.NCCC(O)=O PDLNHDSYGLTYDS-UHFFFAOYSA-N 0.000 claims 1
- 108010008488 Glycylglycine Proteins 0.000 claims 1
- JRIZSBGDMDSKRF-DEGSGYPDSA-N [(2s,3s,4s,5s)-5-(6-aminopurin-9-yl)-3,4-diphosphonooxyoxolan-2-yl]methyl dihydrogen phosphate Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1O[C@@H](COP(O)(O)=O)[C@H](OP(O)(O)=O)[C@@H]1OP(O)(O)=O JRIZSBGDMDSKRF-DEGSGYPDSA-N 0.000 claims 1
- CBTVGIZVANVGBH-UHFFFAOYSA-N aminomethyl propanol Chemical compound CC(C)(N)CO CBTVGIZVANVGBH-UHFFFAOYSA-N 0.000 claims 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 claims 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 claims 1
- 235000011130 ammonium sulphate Nutrition 0.000 claims 1
- 229940043257 glycylglycine Drugs 0.000 claims 1
- 238000012360 testing method Methods 0.000 abstract description 13
- 238000005859 coupling reaction Methods 0.000 abstract description 7
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- 102000004190 Enzymes Human genes 0.000 abstract description 5
- 108090000790 Enzymes Proteins 0.000 abstract description 5
- 239000000463 material Substances 0.000 abstract description 3
- 238000005516 engineering process Methods 0.000 abstract description 2
- 238000010339 medical test Methods 0.000 abstract description 2
- 238000002156 mixing Methods 0.000 abstract description 2
- 229930195712 glutamate Natural products 0.000 abstract 2
- KPGXRSRHYNQIFN-UHFFFAOYSA-N 2-oxoglutaric acid Chemical compound OC(=O)CCC(=O)C(O)=O KPGXRSRHYNQIFN-UHFFFAOYSA-N 0.000 abstract 1
- 102000003960 Ligases Human genes 0.000 abstract 1
- 108090000364 Ligases Proteins 0.000 abstract 1
- 238000002835 absorbance Methods 0.000 abstract 1
- 238000003745 diagnosis Methods 0.000 abstract 1
- 239000000376 reactant Substances 0.000 abstract 1
- 239000003381 stabilizer Substances 0.000 abstract 1
- XTWYTFMLZFPYCI-KQYNXXCUSA-N 5'-adenylphosphoric acid Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O XTWYTFMLZFPYCI-KQYNXXCUSA-N 0.000 description 7
- XTWYTFMLZFPYCI-UHFFFAOYSA-N Adenosine diphosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(O)=O)C(O)C1O XTWYTFMLZFPYCI-UHFFFAOYSA-N 0.000 description 7
- 230000008878 coupling Effects 0.000 description 6
- 238000010168 coupling process Methods 0.000 description 6
- 238000010521 absorption reaction Methods 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 238000001976 enzyme digestion Methods 0.000 description 3
- 101710169336 5'-deoxyadenosine deaminase Proteins 0.000 description 2
- FTOAOBMCPZCFFF-UHFFFAOYSA-N 5,5-diethylbarbituric acid Chemical compound CCC1(CC)C(=O)NC(=O)NC1=O FTOAOBMCPZCFFF-UHFFFAOYSA-N 0.000 description 2
- 102000055025 Adenosine deaminases Human genes 0.000 description 2
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 2
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 2
- 238000009792 diffusion process Methods 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 150000002460 imidazoles Chemical class 0.000 description 2
- 238000005342 ion exchange Methods 0.000 description 2
- 150000002500 ions Chemical class 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 238000012544 monitoring process Methods 0.000 description 2
- 238000006491 synthase reaction Methods 0.000 description 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- VXEQGQXRKQSAMW-UHFFFAOYSA-N 2-amino-2-methylpropan-1-ol Chemical compound CC(C)(N)CO.CC(C)(N)CO VXEQGQXRKQSAMW-UHFFFAOYSA-N 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- PGXABRVTTLRYCN-UHFFFAOYSA-N Cl.Cl.Cl.Cl.C(=O)(O)CCN Chemical compound Cl.Cl.Cl.Cl.C(=O)(O)CCN PGXABRVTTLRYCN-UHFFFAOYSA-N 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- YTNIXZGTHTVJBW-SCRDCRAPSA-N FMNH2 Chemical compound OP(=O)(O)OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C=2C=C(C)C(C)=CC=2NC2=C1NC(=O)NC2=O YTNIXZGTHTVJBW-SCRDCRAPSA-N 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- ZQYUHRVUJCLGRX-UHFFFAOYSA-N NCC(=O)NCC(O)=O.NCC(=O)NCC(O)=O Chemical compound NCC(=O)NCC(O)=O.NCC(=O)NCC(O)=O ZQYUHRVUJCLGRX-UHFFFAOYSA-N 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
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- GHXRKGHKMRZBJH-UHFFFAOYSA-N boric acid Chemical compound OB(O)O.OB(O)O GHXRKGHKMRZBJH-UHFFFAOYSA-N 0.000 description 1
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- BHQCQFFYRZLCQQ-OELDTZBJSA-N cholic acid Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 BHQCQFFYRZLCQQ-OELDTZBJSA-N 0.000 description 1
- 239000007979 citrate buffer Substances 0.000 description 1
- 229940111685 dibasic potassium phosphate Drugs 0.000 description 1
- ZPWVASYFFYYZEW-UHFFFAOYSA-L dipotassium hydrogen phosphate Chemical compound [K+].[K+].OP([O-])([O-])=O ZPWVASYFFYYZEW-UHFFFAOYSA-L 0.000 description 1
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
- 229910000397 disodium phosphate Inorganic materials 0.000 description 1
- 235000019800 disodium phosphate Nutrition 0.000 description 1
- 238000003912 environmental pollution Methods 0.000 description 1
- VWWQXMAJTJZDQX-UYBVJOGSSA-N flavin adenine dinucleotide Chemical compound C1=NC2=C(N)N=CN=C2N1[C@@H]([C@H](O)[C@@H]1O)O[C@@H]1CO[P@](O)(=O)O[P@@](O)(=O)OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C2=NC(=O)NC(=O)C2=NC2=C1C=C(C)C(C)=C2 VWWQXMAJTJZDQX-UYBVJOGSSA-N 0.000 description 1
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- 239000008103 glucose Substances 0.000 description 1
- 229960001031 glucose Drugs 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-M glutaminate Chemical compound [O-]C(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-M 0.000 description 1
- ICIWUVCWSCSTAQ-UHFFFAOYSA-M iodate Chemical compound [O-]I(=O)=O ICIWUVCWSCSTAQ-UHFFFAOYSA-M 0.000 description 1
- FZWBNHMXJMCXLU-BLAUPYHCSA-N isomaltotriose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1OC[C@@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@@H](OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C=O)O1 FZWBNHMXJMCXLU-BLAUPYHCSA-N 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
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- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 238000011430 maximum method Methods 0.000 description 1
- 229910052753 mercury Inorganic materials 0.000 description 1
- QVLTXCYWHPZMCA-UHFFFAOYSA-N po4-po4 Chemical compound OP(O)(O)=O.OP(O)(O)=O QVLTXCYWHPZMCA-UHFFFAOYSA-N 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
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Landscapes
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Abstract
The invention is about a method of measuring the content of blood ammonia, and it also concerns the reagent box of blood ammonia diagnosis. This invention belongs to the field of medical testing and measuring technology. The reagent box is consisted of buffer solution, glutamate, 2-ketoglutarate, reduced coenzyme, adenosine triphosphate, glutamine synthetase, glutamate synthetase and stabilizer. Firstly, we cause an enzyme-coupled reaction through mixing the sample and the reagent according to a certain proportion of volume; secondly, put the final reactant under the biochemical analyzer and test the absorbance variational situation (speed) of dominant wavelength; then we can get the content of blood ammonia. By using this invention, we can get the necessary measuring result with high sensitiveness and fine precision through biochemical analyzer, and the result would not be contaminated by material of internal and exogenous sources. Thus, this method can be conveniently promoted and applied.
Description
Technical field
The present invention relates to a kind of method of measuring blood ammonia content, the invention still further relates to the blood ammonia diagnostic kit simultaneously, belong to medical test determination techniques field.
Background technology
The ammonia method for measuring has microdiffusion, ion exchange method, enzyme process and ammonia electrode method etc.Use at present maximum methods and be enzyme process and based on the determination of blood ammonia instrument analytical method of ion selective electrode.
Diffusion process discharges NH after being the sample alkalization
3, the ammonia that discharges with acidometric titration, or form the two mercury amine of pale brown look iodate with the Nessler reaction and carry out colorimetric.These methods need alkalization, and endogenic ammonia forms and impacts, and its accuracy and precision are affected, and seldom use at present; Ion exchange method is more accurate than diffusion process, and CV is 8%--13%; Ion selective electrode method is to utilize NH
3Be diffused into electrode surface, the PH that causes electrode changes and measures, and the CV of this method is 3.5%--4.8%, rate of recovery height, but all need special instrument, be not suitable for the concrete reality of China.
The retrieval Chinese patent is only found No. 87105593.7 patent applications and is disclosed a kind of rapid freezing cup for blood ammonia determination, does not but find more satisfactory determination of blood ammonia method.
Summary of the invention
The technical problem to be solved in the present invention is: propose a kind of blood ammonia Determination on content method that can overcome above prior art shortcoming, provide simultaneously in order to realize the blood ammonia diagnostic kit of the inventive method.Adopt the reagent in this test kit not only can measure, and finding speed is fast, accuracy is high, thereby can obtains practical applying at ultraviolet analyser or half, the enterprising promoting circulation of blood ammonia content of automatic clinical chemistry analyzer.
It is as follows that the present invention measures the method steps of blood ammonia content:
1), with sample and the reagent mix of mainly forming by L-glutamic acid, 2-oxoglutaric acid ester, reduced coenzyme, adenosine triphosphate, glutamine synthetase, NADPH-linked glutamate synthase, make it to take place the reaction of following principle:
Adenosine triphosphate+L-glutamic acid+ammonia
Glutamine synthetaseAdenosine diphosphate (ADP)+
Phosphate radical+glutamine
Glutamine+2-oxoglutaric acid ester+reduced coenzyme
NADPH-linked glutamate synthase
L-glutamic acid+oxidized coenzyme
2), detect the end reaction thing in predominant wavelength 340nm absorbancy decline scope, calculate the content of blood ammonia.
Common step 2) the end reaction thing is placed under ultraviolet analyser or half, the automatic clinical chemistry analyzer device, detect the degree that predominant wavelength 340nm absorbancy descends, calculate the content of blood ammonia.
The blending ratio of above sample and reagent is by volume 1/10 to 1/250, and the mensuration temperature of above process is controlled at 20 ℃ to 50 ℃ conventional scopes, and the reaction times was controlled at conventional 2-30 minute.
This method is used glutamine synthetase coupling NADPH-linked glutamate synthase reaction continuous monitoring method.Ammonia is by the effect of coupling glutamine synthetase, generate glutamine with adenosine triphosphate and L-glutamic acid, glutamine is the effect by the coupling NADPH-linked glutamate synthase again, reduced coenzyme (absorption peak being arranged at the 340nm place) is oxidized into coenzyme (not having absorption peak at the 340nm place), thereby measured the speed that reduced coenzyme descends in 340nm place absorbancy, by measuring the speed that 340nm place absorbancy descends, can calculate the active size of adenosine deaminase.
Be used to realize that the blood ammonia diagnostic kit of the inventive method can be single agent, comprise:
Damping fluid 40--200mmol/l
L-glutamic acid 1--30mmol/l
20-ALPHA-KG 1--50mmol/l
Reduced coenzyme 0.15--0.3mmo/l
Adenosine triphosphate 1--10mmol/l
Glutamine synthetase 1000--50000U/l
NADPH-linked glutamate synthase 1000--50000U/l
Stablizer 10--80% (cumulative volume)
Also above single agent can be made into following pair of agent:
Reagent I
Damping fluid 40--200mmol/l
L-glutamic acid 1--30mmol/l
2-oxoglutaric acid ester 1--50mmol/l
Reduced coenzyme 0.15--0.3mmo/l
Adenosine triphosphate 1--10mmol/l
NADPH-linked glutamate synthase 1000--50000U/l
Stablizer 10--80% (cumulative volume)
Reagent II
Damping fluid 40--200mmol/l
Glutamine synthetase 1000--50000U/l
Stablizer 10--80% (cumulative volume)
The prescription of two agent is not limited only to above-mentioned prescription, the composition of reagent I wherein, L-glutamic acid, 2-oxoglutaric acid ester, reduced coenzyme, adenosine triphosphate, NADPH-linked glutamate synthase etc. can be placed on reagent II, reagent II composition wherein, glutamine synthetase also can be placed on reagent I, so can form multiple formulations, not describe in detail one by one at this.
Reagent can also be made into following three reagent, more help the stable of reagent:
Reagent I
Damping fluid 40--200mmol/l
L-glutamic acid 1--30mmol/l
2-oxoglutaric acid ester 1--50mmol/l
Reduced coenzyme 0.15--0.3mmo/l
Adenosine triphosphate 1--10mmol/l
Stablizer 10--50mmol/l
Reagent II
Damping fluid 40--200mmol/l
NADPH-linked glutamate synthase 1000--50000U/l
Stablizer 10--80% (cumulative volume)
Reagent III
Damping fluid 40--200mmol/l
Glutamine synthetase 1000--50000U/l
Stablizer 10--80% (cumulative volume)
Three doses prescription is not limited only to above-mentioned prescription, the composition of reagent I wherein, and L-glutamic acid, 2-oxoglutaric acid ester, reduced coenzyme, adenosine triphosphate etc. can be placed among reagent II or the reagent III.Reagent II composition wherein, NADPH-linked glutamate synthase also can be placed among reagent I or the reagent III, and reagent III composition wherein, glutamine synthetase also can be placed among reagent I or the reagent II, so can form multiple formulations, do not describe in detail one by one at this.
The pH scope of buffer reagent can be 6.0～11.0.Buffer reagent can be three (carboxymethyl) aminomethane-hydrochloric acid (Tris-HCl) damping fluid, phosphoric acid salt (Phosphate) damping fluid, trolamine (Triethanolamine) damping fluid, 2-amino-2-methyl-1-propanol (2-Amino-2-methyl-1-propanol) damping fluid, imidazoles (Imidazole) damping fluid or glycylglycine (Glycylglycine) damping fluid etc., (for example can also be imidazoles/hydrochloride buffer 6.2-7.8 but be not limited only to these damping fluids; Sodium phosphate dibasic citrate buffer solution 5.0-8.0; Citric acid sodium citrate buffer solution 5.0-6.6; Phosphate buffered saline buffer 6.0-8.0; Sodium phosphate dibasic-potassium phosphate buffer 6.0-8.0; Potassium primary phosphate sodium hydrate buffer solution 6.0-8.0; Veronal sodium-hydrochloride buffer 6.8-9.6; Tris hydrochloride buffer 7.0-9.0; Boric acid borate buffer solution 7.4-9.0; Glycine-sodium hydrate buffer solution 8.6-10.6; Sand-sodium hydrate buffer solution 9.2-10.0; Yellow soda ash-sodium bicarbonate buffer liquid 8.8-10.6 (Ca
2+, Mg
2+Must not use when existing); PBS damping fluid 7.0-7.6 etc.).
Above reduced coenzyme can be reduced form nicotinamide coenzyme or derivatives thereofs such as NADPH, NADH or thio-NADH.
In addition, in order to reduce the cross influence between each reagent composition, the stability that keeps reagent, so that standing storage, above single agent, the reagent I of two agent, the reagent I of reagent II or three doses, reagent II, usually add stablizer 10～80% or 10～50mmol/l among the reagent III, stablizer can be an ethylene glycol, propylene glycol, glycerine, glycan, polyalcohols, in sulfuric acid amine or the salt etc. one or more can also be at thioglycol, adenosine diphosphate (ADP), bovine serum albumin, carbonate, cholate, dextran, ethylenediamine tetraacetic acid (EDTA), flavin adenine dinucleotide, vitamin B2 phosphate, glucose, glutaminate, lactose, N.F,USP MANNITOL, sucrose, sodium-chlor, select in the succinate etc.
Experiment shows, takes all factors into consideration from the accuracy of measurement result and economy two aspects of preparation cost, no matter is single agent, two agent or three doses, and the blood ammonia diagnostic kit of the present invention of following system component relation is comparatively desirable:
Damping fluid 80--120mmol/l
L-glutamic acid 5--10mmol/l
2-oxoglutaric acid ester 5--20mmol/l
Reduced coenzyme 0.2--0.3mmol/l
Adenosine triphosphate 2--8mmol/l
Glutamine synthetase 4000--10000U/l
NADPH-linked glutamate synthase 4000--10000U/l
Stablizer 20--50% (cumulative volume)
Because the present invention utilizes Enzymology method, enzyme digestion reaction to have the high characteristics of specificity fully, is not vulnerable to the interference of other materials of inside and outside source.Easy, the easy handling of enzyme process method.The specificity of enzyme digestion reaction impels test result accurate.Enzyme digestion reaction all is to carry out under buffer conditions, does not have environmental pollution problem.The enzyme process method does not need special, extra instrument, and testing cost is cheap.Therefore can guarantee to have higher test accuracy, be more convenient for applying.
Embodiment
The present invention is further illustrated below in conjunction with examples of implementation.
Embodiment one (single agent)
The blood ammonia diagnostic kit of present embodiment comprises:
Damping fluid 80mmol/l
L-glutamic acid 5mmol/l
2-oxoglutaric acid ester 5mmol/l
Reduced coenzyme 0.2mmo/l
Adenosine triphosphate 2mmol/l
Glutamine synthetase 4000U/l
NADPH-linked glutamate synthase 4000U/l
Stablizer 50% (cumulative volume)
On automatic clinical chemistry analyzer, set: 37 ℃ of temperature, 10 minutes reaction times, test predominant wavelength 340nm, more than the test commplementary wave length 405nm, the volume ratio of tested blood ammonia sample and reagent is 1/25, the Direction of Reaction is negative reaction.
After adding sample and reagent, make it to mix, following reaction take place:
Adenosine triphosphate+L-glutamic acid+ammonia
Glutamine synthetaseAdenosine diphosphate (ADP)+
Phosphate radical+glutamine
Glutamine+2-oxoglutaric acid ester+reduced coenzyme
NADPH-linked glutamate synthase
L-glutamic acid+oxidized coenzyme
The end reaction thing is placed under the biochemical analyzer, detect predominant wavelength 340nm absorbancy decline scope, thereby calculate the content of blood ammonia.
Present embodiment is used glutamine synthetase coupling NADPH-linked glutamate synthase reaction continuous monitoring method.Ammonia is by the effect of coupling glutamine synthetase, generate glutamine with adenosine triphosphate and L-glutamic acid, glutamine is the effect by the coupling NADPH-linked glutamate synthase again, reduced coenzyme (absorption peak being arranged at the 340nm place) is oxidized into coenzyme (not having absorption peak at the 340nm place), thereby measured the speed that reduced coenzyme descends in 340nm place absorbancy, by measuring the speed that 340nm place absorbancy descends, can calculate the active size of adenosine deaminase.
Embodiment two (two agent)
The blood ammonia diagnostic reagent of present embodiment has:
Reagent I
Damping fluid 100mmol/l
L-glutamic acid 8mmol/l
2-oxoglutaric acid ester 12mmol/l
Reduced coenzyme 0.25mmo/l
Adenosine triphosphate 5mmol/l
NADPH-linked glutamate synthase 7000U/l
Stablizer 50% (cumulative volume)
Reagent II
Damping fluid 100mmol/l
Glutamine synthetase 7000U/l
Stablizer 50% (cumulative volume)
When measuring blood ammonia content, temperature is controlled at 30 ℃, 15 minutes reaction times, and test predominant wavelength 340nm, more than the test commplementary wave length 405nm, the volume ratio of tested blood ammonia sample and reagent is 1/25, the Direction of Reaction is negative reaction.
Concrete determination step is:
Adenosine triphosphate+L-glutamic acid+ammonia
Glutamine synthetaseAdenosine diphosphate (ADP)+
Phosphate radical+glutamine
Glutamine+2-oxoglutaric acid ester+reduced coenzyme
NADPH-linked glutamate synthase
L-glutamic acid+oxidized coenzyme
The end reaction thing is placed under the biochemical analyzer, detect predominant wavelength 340nm absorbancy decline scope, thereby calculate the content of blood ammonia.
The reaction times of each reactions steps was controlled at 15 minutes.
Embodiment three (three doses)
The blood ammonia diagnostic reagent of present embodiment is three doses, has:
Reagent I
Damping fluid 120mmol/l
L-glutamic acid 10mmol/l
2-oxoglutaric acid ester 20mmol/l
Reduced coenzyme 0.3mmo/l
Adenosine triphosphate 8mmol/l
Stablizer 20mmol/l
Reagent II
Damping fluid 120mmol/l
NADPH-linked glutamate synthase 10000U/l
Stablizer 50% (cumulative volume)
Reagent III
Damping fluid 120mmol/l
Glutamine synthetase 10000U/l
Stablizer 50% (cumulative volume)
On automatic clinical chemistry analyzer, set: 25 ℃ of temperature, 20 minutes reaction times, test predominant wavelength 340nm, more than the test commplementary wave length 405nm, the volume ratio of tested blood ammonia sample and reagent is 1/25, the Direction of Reaction is negative reaction.
Concrete determination step is:
Adenosine triphosphate+L-glutamic acid+ammonia
Glutamine synthetaseAdenosine diphosphate (ADP)+
Phosphate radical+glutamine
Glutamine+2-oxoglutaric acid ester+reduced coenzyme
NADPH-linked glutamate synthase
L-glutamic acid+oxidized coenzyme
The end reaction thing is placed under the biochemical analyzer, detect predominant wavelength 340nm absorbancy decline scope, thereby calculate the content of blood ammonia.
The reaction times of each reactions steps was controlled at 20 minutes.
Embodiment four
The blood ammonia diagnostic reagent of present embodiment has:
Reagent I
Damping fluid 100mmol/l
L-glutamic acid 5mmol/l
2-oxoglutaric acid ester 12mmol/l
Reduced coenzyme 0.3mmo/l
Adenosine triphosphate 2mmol/l
Stablizer 20mmol/l
Reagent II
Damping fluid 100mmol/l
Glutamine synthetase 10000U/l
NADPH-linked glutamate synthase 10000U/l
Stablizer 50% (cumulative volume)
On Biochemical Analyzer, set: 37 ℃ of temperature, 10 minutes reaction times, test predominant wavelength 340nm, more than the test commplementary wave length 405nm, the volume ratio of tested blood ammonia sample and reagent is 1/25, the Direction of Reaction is negative reaction.
After adding sample and reagent, make it to mix, following reaction take place:
Adenosine triphosphate+L-glutamic acid+ammonia
Glutamine synthetaseAdenosine diphosphate (ADP)+
Phosphate radical+glutamine
Glutamine+2-oxoglutaric acid ester+reduced coenzyme
NADPH-linked glutamate synthase
L-glutamic acid+oxidized coenzyme
The end reaction thing is placed under the biochemical analyzer, detect predominant wavelength 340nm absorbancy decline scope, thereby calculate the content of blood ammonia.
In a word, experiment showed, and adopt measuring method of the present invention can draw required measurement result by ultraviolet analyser or half, automatic clinical chemistry analyzer device fully, and highly sensitive, tolerance range good, is not subjected to the pollution of inside and outside source material.
Claims (9)
1. method of measuring blood ammonia content, step is as follows:
1), with sample and the reagent mix of mainly forming by L-glutamic acid, 2-oxoglutaric acid ester, reduced coenzyme, adenosine triphosphate, glutamine synthetase, NADPH-linked glutamate synthase, make it to take place the reaction of following principle:
Adenosine triphosphate+L-glutamic acid+ammonia
Glutamine synthetaseAdenosine diphosphate (ADP)+
Phosphate radical+glutamine
Glutamine+2-oxoglutaric acid ester+reduced coenzyme
NADPH-linked glutamate synthase
L-glutamic acid+oxidized coenzyme
2), detect the end reaction thing in predominant wavelength 340nm absorbancy decline scope, calculate the content of blood ammonia.
2. according to the method for the described mensuration blood ammonia of claim 1 content, it is characterized in that: described step 2) for the end reaction thing being placed under ultraviolet analyser or half, the automatic clinical chemistry analyzer, detect the degree that predominant wavelength 340nm absorbancy descends, calculate the content of blood ammonia.
3, according to the method for claim 1 or 2 described mensuration blood ammonia content, it is characterized in that: temperature is controlled at 20 ℃ to 50 ℃ scopes, and the reaction times was controlled at 2-30 minute.
4, according to the method for claim 1 or 2 described mensuration blood ammonia content, it is characterized in that: the ratio control of sample and reagent is 1/10 to 1/250.
5. blood ammonia diagnostic kit is grouped into by following one-tenth:
Damping fluid 40--200mmol/l
L-glutamic acid 1--30mmol/l
2-oxoglutaric acid ester 1--50mmol/l
Reduced coenzyme 0.15--0.3mmo/l
Adenosine triphosphate 1--10mmol/l
Glutamine synthetase 1000--50000U/l
NADPH-linked glutamate synthase 1000--50000U/l
Stablizer 10--80% (cumulative volume)
6. according to the described blood ammonia diagnostic kit of claim 5, it is characterized in that: described reagent is made into single agent, two agent or three doses.
7. according to claim 5 or 6 described blood ammonia diagnostic kits, it is characterized in that: described stablizer is at least a in ethylene glycol, propylene glycol, glycerine, glycan, polyalcohols, ammonium sulfate or the salt.
8. according to claim 5 or 6 described blood ammonia diagnostic kits, it is characterized in that: the pH scope of described buffer reagent is 6.0～11.0, and described buffer reagent is a kind of in three (carboxymethyl) aminomethane-hydrochloride buffer, phosphate buffered saline buffer, trolamine damping fluid, 2-amino-2-methyl-1-propanol damping fluid, imidazole buffer or the glycylglycine damping fluid.
9, according to claim 5 or 6 described blood ammonia diagnostic kits, it is characterized in that: described reduced coenzyme is a kind of in NADPH, NADH or the thio-NADH reduced form nicotinamide coenzyme or derivatives thereof.
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|---|---|---|---|
| CN 200410065557 CN1778937A (en) | 2004-11-23 | 2004-11-23 | Determination of blood ammonia content and blood ammonia diagnostic reagent kit |
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| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN 200410065557 CN1778937A (en) | 2004-11-23 | 2004-11-23 | Determination of blood ammonia content and blood ammonia diagnostic reagent kit |
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Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102298036A (en) * | 2010-06-25 | 2011-12-28 | 苏州艾杰生物科技有限公司 | Method for determining glycine and glycine determination kit |
| CN113075139A (en) * | 2021-03-29 | 2021-07-06 | 迪瑞医疗科技股份有限公司 | Stable double-reagent blood ammonia determination kit |
-
2004
- 2004-11-23 CN CN 200410065557 patent/CN1778937A/en active Pending
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102298036A (en) * | 2010-06-25 | 2011-12-28 | 苏州艾杰生物科技有限公司 | Method for determining glycine and glycine determination kit |
| CN113075139A (en) * | 2021-03-29 | 2021-07-06 | 迪瑞医疗科技股份有限公司 | Stable double-reagent blood ammonia determination kit |
| CN113075139B (en) * | 2021-03-29 | 2022-10-11 | 迪瑞医疗科技股份有限公司 | Stable double-reagent blood ammonia determination kit |
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