IL38918A - Process for the specific enzymatic determination of creatinine and reagent therefor - Google Patents
Process for the specific enzymatic determination of creatinine and reagent thereforInfo
- Publication number
- IL38918A IL38918A IL38918A IL3891872A IL38918A IL 38918 A IL38918 A IL 38918A IL 38918 A IL38918 A IL 38918A IL 3891872 A IL3891872 A IL 3891872A IL 38918 A IL38918 A IL 38918A
- Authority
- IL
- Israel
- Prior art keywords
- creatinine
- creatine
- process according
- specific determination
- determined
- Prior art date
Links
- DDRJAANPRJIHGJ-UHFFFAOYSA-N creatinine Chemical compound CN1CC(=O)NC1=N DDRJAANPRJIHGJ-UHFFFAOYSA-N 0.000 title claims description 70
- 229940109239 creatinine Drugs 0.000 title claims description 35
- 238000000034 method Methods 0.000 title claims description 31
- 239000003153 chemical reaction reagent Substances 0.000 title claims description 11
- 230000002255 enzymatic effect Effects 0.000 title description 2
- CVSVTCORWBXHQV-UHFFFAOYSA-N creatine Chemical compound NC(=[NH2+])N(C)CC([O-])=O CVSVTCORWBXHQV-UHFFFAOYSA-N 0.000 claims description 32
- 229960003624 creatine Drugs 0.000 claims description 16
- 239000006046 creatine Substances 0.000 claims description 16
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 12
- 239000000872 buffer Substances 0.000 claims description 12
- 108010066906 Creatininase Proteins 0.000 claims description 10
- 108010077078 Creatinase Proteins 0.000 claims description 8
- 238000006243 chemical reaction Methods 0.000 claims description 8
- 102000004420 Creatine Kinase Human genes 0.000 claims description 6
- 108010042126 Creatine kinase Proteins 0.000 claims description 6
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 claims description 6
- OXNIZHLAWKMVMX-UHFFFAOYSA-N picric acid Chemical compound OC1=C([N+]([O-])=O)C=C([N+]([O-])=O)C=C1[N+]([O-])=O OXNIZHLAWKMVMX-UHFFFAOYSA-N 0.000 claims description 6
- 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 description 5
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims description 4
- 230000015572 biosynthetic process Effects 0.000 claims description 4
- DTBNBXWJWCWCIK-UHFFFAOYSA-N phosphoenolpyruvic acid Chemical compound OC(=O)C(=C)OP(O)(O)=O DTBNBXWJWCWCIK-UHFFFAOYSA-N 0.000 claims description 4
- 102000003855 L-lactate dehydrogenase Human genes 0.000 claims description 3
- 108700023483 L-lactate dehydrogenases Proteins 0.000 claims description 3
- 102000013009 Pyruvate Kinase Human genes 0.000 claims description 3
- 108020005115 Pyruvate Kinase Proteins 0.000 claims description 3
- 239000004202 carbamide Substances 0.000 claims description 3
- 229910001629 magnesium chloride Inorganic materials 0.000 claims description 3
- 238000005259 measurement Methods 0.000 claims description 3
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 claims description 3
- 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 3
- 239000000243 solution Substances 0.000 claims description 3
- 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 description 2
- 229910019142 PO4 Inorganic materials 0.000 claims description 2
- 239000007864 aqueous solution Substances 0.000 claims description 2
- XPPKVPWEQAFLFU-UHFFFAOYSA-J diphosphate(4-) Chemical compound [O-]P([O-])(=O)OP([O-])([O-])=O XPPKVPWEQAFLFU-UHFFFAOYSA-J 0.000 claims description 2
- 235000011180 diphosphates Nutrition 0.000 claims description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 claims description 2
- 239000010452 phosphate Substances 0.000 claims description 2
- 229930029653 phosphoenolpyruvate Natural products 0.000 claims description 2
- 230000026731 phosphorylation Effects 0.000 claims description 2
- 238000006366 phosphorylation reaction Methods 0.000 claims description 2
- 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 claims 1
- 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 claims 1
- ZKHQWZAMYRWXGA-KQYNXXCUSA-N Adenosine triphosphate 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-N 0.000 claims 1
- 241000975394 Evechinus chloroticus Species 0.000 claims 1
- 238000011534 incubation Methods 0.000 claims 1
- 230000008033 biological extinction Effects 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 210000002966 serum Anatomy 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 230000035945 sensitivity Effects 0.000 description 3
- 239000004471 Glycine Substances 0.000 description 2
- 238000007375 Jaffe assay Methods 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- OIRDTQYFTABQOQ-KQYNXXCUSA-N adenosine Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O OIRDTQYFTABQOQ-KQYNXXCUSA-N 0.000 description 2
- 238000011835 investigation Methods 0.000 description 2
- FSYKKLYZXJSNPZ-UHFFFAOYSA-N sarcosine Chemical compound C[NH2+]CC([O-])=O FSYKKLYZXJSNPZ-UHFFFAOYSA-N 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 1
- 239000002126 C01EB10 - Adenosine Substances 0.000 description 1
- 244000026610 Cynodon dactylon var. affinis Species 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- JVTAAEKCZFNVCJ-UHFFFAOYSA-M Lactate Chemical compound CC(O)C([O-])=O JVTAAEKCZFNVCJ-UHFFFAOYSA-M 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- LCTONWCANYUPML-UHFFFAOYSA-M Pyruvate Chemical compound CC(=O)C([O-])=O LCTONWCANYUPML-UHFFFAOYSA-M 0.000 description 1
- 108010077895 Sarcosine Proteins 0.000 description 1
- VZOHDTADJSIIAP-UHFFFAOYSA-M [Hg]SC#N.[K] Chemical compound [Hg]SC#N.[K] VZOHDTADJSIIAP-UHFFFAOYSA-M 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 229960005305 adenosine Drugs 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 239000000287 crude extract Substances 0.000 description 1
- 238000006073 displacement reaction Methods 0.000 description 1
- 239000007999 glycylglycine buffer Substances 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-M hydroxide Chemical compound [OH-] XLYOFNOQVPJJNP-UHFFFAOYSA-M 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 229940043230 sarcosine Drugs 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/34—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving hydrolase
-
- 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
- G01N33/70—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving creatine or creatinine
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Organic Chemistry (AREA)
- Molecular Biology (AREA)
- Physics & Mathematics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Analytical Chemistry (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- Pathology (AREA)
- General Physics & Mathematics (AREA)
- Food Science & Technology (AREA)
- Cell Biology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Description
TO PROCESS FOR THE SPECIFIC ENZYMATIC OP CREATININE THER OR The present invention is with a new process and with a reagent the specific determinatio of In clinical especially for functional kidney the determination of creatinine plays an important The determination of creatinine in the serum in the clearance the simultaneous determination in the serum and is one of the standar methods of investigation used in clinical the determination of the creatinine content of certain foodstuffs and animal feeds is also of The method of determination previously used depends upon the colour found by of creatinine with picric acid in an alkaline After acidic proteinisation of the sample for acetic acid or picric in the supernatant there is after the addition of picric acid and a which is measured An important disadvantage of this simple method however that it is not specific for A number of modifications of the Jaffe reaction admittedly improve the degree of precision and the carryin out thereof but without removing this principal The Jaffe method remains very subject to disturbance and even slight displacements in the hydrogen or hydroxyl ion concentration result in an alteration of the colour According to another known creatinine is with the addition of into which is then determined by the Sakaguchi a colour reaction between creatinine and potassium mercury thiocyanate has also been both methods prove to be unsuitable for use clinical A of the Jaffe reaction has been cribed by Dubos and Miller in using crude extract of a certain creatinine is decomposed in an aliguot of a whereas the remainder of the sample remains In both parts of a creatinine determination is carried out by s method and the creatinine content determined from the difference of the This method is admittedly very specific but it is very laborious to carry out and the bacterium used has to be continuously there is a need for a simple but specific test for the determination of According to the present there is provided a process for the specific determination of wherein an aqueous solution is incubated with creatinine amidohydrolase at a pH value between about and 9 and either the creatine formed or the decrease of creatinine is determined in known The enzyme creatinine amidohydrolase used for the process according to the present invention not been catalyses the creatinine creatinine E O creatine The creatine can be measured directly by known for by phosphorylation with creati kinase and adenosine triphosphate with the formation of adenosine which is determined in Another possibility is to measure the decrease of the creatinine content by The process according to the present invention is preferably carried out at a pH value between and For the adjustment of the pH any desired buffers can be care is to be taken that the buffer used does not disturb the subsequent method of for the creatinine difference is subsequently to be determined by the buffe used should not diminish the Jaffe Glycine and glycylglycine buffers for wherea phosphate and pyrophosphate buffers do not have a disturbi the creatine formed is to be mined with creatine kinase and then glycine buffer and similar buffers can also be For carrying out the process according to the presen a previous deproteinisation of the sample is no a deproteinisation can be expedient for the subsequent determination of the According to a preferred embodiment of the process according to the present creatine formed is with the use of the enzyme into sarcosine and urea and the latter determined according to known The enzyme creatinase is also described in our copending Application and can systematically also be classified as creatine This preferred embodiment of the process according to the present invention is preferably carried out by using for the determination an enzyme preparation ing a mixture of creatininase and If the creatine formed is determined in known with the use of creatinase and then a deproteinisation is advantageous since the sensitivity of the test is thereb This greater sensitivity depends upon the fact in the case of it is possible to work in a more concentrated form so that the extinction referred to a certain amount of is The use of an enzyme mixture containing creatinine amidohydrolase and creatinase is also of advantage when the determination of the creatinine is carried out by method due to the presence of the the equilibrium is displaced in favour of the formation of The present invention also provides a new reagent combination for the specific determination of The reagent combination according to the present invention a creatinine standard picric acid an agueous solution of sodium hydroxide and creatinine amidohydrolase alone or together with buffer and optionally in admixture with creatinase in an unmixed state before A further reagent combination according to the presen invention a reduced ATP and phosphoenol pyruvate lactate dehydrogenase pyruvate kinase and magnesium chloride creatine kinase and creatinine in an unmixed state The process according to the present invention and reagent combinations according to the present invention for the first the possibility of carrying out a specific creatinine determination which can also be used routinely in clinical laboratories and possesses a sufficient degree of sensitivity for practical The only previously known specific method for the ation of creatinine according to Miller and be used for routine investigations Clinical page The following Examples are given for the purpose of illustrating the present Example Determination of creatinine with subsequent use of the Jaffe of a sample or diluted is incubated at for to 60 minutes in to buffer preferred buffers are acid or acid with creatinine amidohydrolase in an amount of at least 1 substrate and creatinase in an amount of at least The test sample is then deproteini with trichloroacetic together with a sample to which enzyme mixture has been The reaction is carried out with the supernatant of the two The extinction difference of the two samples at 5 nm gives the amount of with reference to a creatinine standard The colour reaction is carried out by adding picric acid and an aqueous sodium hydroxide leaving to stand for 15 minutes at ambient temperature and measuring in a cuvette with 2 layer thickness at 546 of the accompanying drawings shows graphically the linearity between of creatinine and the extinction difference at 546 Example Measurement of creatine by means of creatine The principle of this embodiment is with the help of the creatinine is hydrolysed to creatine and the creatine formed is using the method described by of with creatine kinase and the formed is converted with PEP and PK into ATP and the pyruvate thereby formed is reduced with NADH and lactate ase to with the formation of The reaction of 1 NADH at 340 or 366 ponds to the presence of 1 mol For carrying out this a reagent which contains PEP and magnesium chloride in M buffer at pH is mixed with lactate dehydrogenase pyruvate kinase and adjusted to Serum and creatine kinase are then added and the mixture incubate for a maximum of minutes at the given the reaction started by the addition of at least 5 creatininase The decrease in extinction is The reaction period is to depending upon the creatinine The creatinine content can calculated directly via the molar extinction coefficients of of the accompanying drawings shows graphically the linearity of this embodiment of the process according to the present Advantages of this embodiment include a saving of test material by a factor of 10 in comparison with the a serum blank is not necessary and on centrif ging are also not insufficientOCRQuality
Claims (12)
1. What we claim is :- 1. A process for the specific determination of creatinin wherein an aqueous, creatinine-contai ing solution is incubated with creatinine amidohydrolase at a pH value' between about 7.5 and 9 and either the creatine formed or the decrease of creatinine is determined in known manner.
2. A process according to claim 1 , wherein the reaction is carried out in a phosphate or pyrophosphate buffer and the creatinine difference is determined by measurement of the coloration formed with picric acid and aqueous sodium hydroxide solution.
3. A process according to claim 1 , wherein the creatine formed is determined by phosphorylation v/ith creatine kinas and adenosine triphosphate and measurement of the adenosine diphosphate formed. k.
4. A process according to claim 1 , wherein the creatine formed is decomposed in the presence of creatinase, with the formation of urea, and the urea formed is determined in known manner.
5. A process according to any of the preceding claims, wherein the incubation reaction is carried out at pH 7.8 to 8.3.
6. A process according to claim 3, wherein the sample to be tested is deproteinised before measuring the creatine with the use of creatine kinase.
7. A process according to any of the preceding claims, wherein the creatinine amidohydrolase is used in admixture with creatinase.
8. A process according to claim 1 for the specific determination of creatinine, substantially as hereinbefore described and exemplified. J■
9. A reagent combination for the specific determination of creatinine, comprising: 1. a creatinine standard 2. picric acid 3. an aqueous solution of sodium hydroxide k. creatinine am dohydrolase alone or together with buffer and optionally in admixture with creatinase, in an unmixed state before use.
10. A reagent combination for the specific determination of creatinine, comprising: 1. buffer, NADH, ATP and phosphoenol pyruvate 2. lactate dehydrogenase, pyruvate kinase and magnesium chloride 3· creatine kinase and k» creatinine amidohydrolase, in an unmixed state before use.
11. A reagent combination according to claim 9 or 10 for the specific determination of creatinine, substantially as hereinbefore described.
12. A process for the specific determination of creatinin whenever carried out with the use of a reagent combination according to any of claims 9 to 11. Attorney f oi Applicants
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE2122255A DE2122255B2 (en) | 1971-05-05 | 1971-05-05 | Method for the specific determination of creatinine |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| IL38918A0 IL38918A0 (en) | 1972-05-30 |
| IL38918A true IL38918A (en) | 1974-12-31 |
Family
ID=5806955
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IL38918A IL38918A (en) | 1971-05-05 | 1972-03-07 | Process for the specific enzymatic determination of creatinine and reagent therefor |
Country Status (8)
| Country | Link |
|---|---|
| JP (1) | JPS5443397B1 (en) |
| DK (1) | DK139769C (en) |
| FI (1) | FI53367C (en) |
| HU (1) | HU163672B (en) |
| IL (1) | IL38918A (en) |
| IT (1) | IT968190B (en) |
| SE (1) | SE377723B (en) |
| SU (1) | SU1144629A3 (en) |
-
1972
- 1972-03-02 IT IT21333/72A patent/IT968190B/en active
- 1972-03-07 IL IL38918A patent/IL38918A/en unknown
- 1972-04-17 SU SU721777222A patent/SU1144629A3/en active
- 1972-05-04 FI FI1265/72A patent/FI53367C/en active
- 1972-05-04 HU HUBO1370A patent/HU163672B/hu unknown
- 1972-05-04 SE SE7205871A patent/SE377723B/xx unknown
- 1972-05-04 DK DK221272A patent/DK139769C/en not_active IP Right Cessation
- 1972-05-06 JP JP4495272A patent/JPS5443397B1/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| DK139769B (en) | 1979-04-09 |
| IT968190B (en) | 1974-03-20 |
| FI53367B (en) | 1977-12-30 |
| SU1144629A3 (en) | 1985-03-07 |
| IL38918A0 (en) | 1972-05-30 |
| JPS5443397B1 (en) | 1979-12-19 |
| SE377723B (en) | 1975-07-21 |
| DK139769C (en) | 1979-09-24 |
| FI53367C (en) | 1978-04-10 |
| HU163672B (en) | 1973-10-27 |
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