SU1144629A3 - Method of determining creatinine in blood serum - Google Patents
Method of determining creatinine in blood serum Download PDFInfo
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- SU1144629A3 SU1144629A3 SU721777222A SU1777222A SU1144629A3 SU 1144629 A3 SU1144629 A3 SU 1144629A3 SU 721777222 A SU721777222 A SU 721777222A SU 1777222 A SU1777222 A SU 1777222A SU 1144629 A3 SU1144629 A3 SU 1144629A3
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- creatinine
- creatine
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- blood serum
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- DDRJAANPRJIHGJ-UHFFFAOYSA-N creatinine Chemical compound CN1CC(=O)NC1=N DDRJAANPRJIHGJ-UHFFFAOYSA-N 0.000 title claims abstract description 55
- 229940109239 creatinine Drugs 0.000 title claims abstract description 28
- 238000000034 method Methods 0.000 title claims abstract description 22
- 210000002966 serum Anatomy 0.000 title claims description 6
- CVSVTCORWBXHQV-UHFFFAOYSA-N creatine Chemical compound NC(=[NH2+])N(C)CC([O-])=O CVSVTCORWBXHQV-UHFFFAOYSA-N 0.000 claims abstract description 34
- 229960003624 creatine Drugs 0.000 claims abstract description 17
- 239000006046 creatine Substances 0.000 claims abstract description 17
- 230000003247 decreasing effect Effects 0.000 claims abstract 2
- 239000008280 blood Substances 0.000 abstract 1
- 210000004369 blood Anatomy 0.000 abstract 1
- 102000004420 Creatine Kinase Human genes 0.000 description 10
- 108010042126 Creatine kinase Proteins 0.000 description 10
- 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 description 8
- 239000000872 buffer Substances 0.000 description 8
- 238000006243 chemical reaction Methods 0.000 description 7
- 102000004190 Enzymes Human genes 0.000 description 6
- 108090000790 Enzymes Proteins 0.000 description 6
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 6
- 108090000604 Hydrolases Proteins 0.000 description 5
- 102000004169 proteins and genes Human genes 0.000 description 5
- 108090000623 proteins and genes Proteins 0.000 description 5
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- 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 description 4
- BAWFJGJZGIEFAR-NNYOXOHSSA-N NAD zwitterion 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](O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 BAWFJGJZGIEFAR-NNYOXOHSSA-N 0.000 description 3
- 230000008033 biological extinction Effects 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 229950006238 nadide Drugs 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 108010077078 Creatinase Proteins 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 102000003855 L-lactate dehydrogenase Human genes 0.000 description 2
- 108700023483 L-lactate dehydrogenases Proteins 0.000 description 2
- JVTAAEKCZFNVCJ-UHFFFAOYSA-M Lactate Chemical compound CC(O)C([O-])=O JVTAAEKCZFNVCJ-UHFFFAOYSA-M 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- LCTONWCANYUPML-UHFFFAOYSA-M Pyruvate Chemical compound CC(=O)C([O-])=O LCTONWCANYUPML-UHFFFAOYSA-M 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- XPPKVPWEQAFLFU-UHFFFAOYSA-J diphosphate(4-) Chemical compound [O-]P([O-])(=O)OP([O-])([O-])=O XPPKVPWEQAFLFU-UHFFFAOYSA-J 0.000 description 2
- 235000011180 diphosphates Nutrition 0.000 description 2
- YMAWOPBAYDPSLA-UHFFFAOYSA-N glycylglycine Chemical compound [NH3+]CC(=O)NCC([O-])=O YMAWOPBAYDPSLA-UHFFFAOYSA-N 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- DTBNBXWJWCWCIK-UHFFFAOYSA-K phosphonatoenolpyruvate Chemical compound [O-]C(=O)C(=C)OP([O-])([O-])=O DTBNBXWJWCWCIK-UHFFFAOYSA-K 0.000 description 2
- 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 description 2
- FSYKKLYZXJSNPZ-UHFFFAOYSA-N sarcosine Chemical compound C[NH2+]CC([O-])=O FSYKKLYZXJSNPZ-UHFFFAOYSA-N 0.000 description 2
- 235000011121 sodium hydroxide Nutrition 0.000 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 description 1
- 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 description 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 description 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 description 1
- 108010008488 Glycylglycine Proteins 0.000 description 1
- 102000006746 NADH Dehydrogenase Human genes 0.000 description 1
- 108010086428 NADH Dehydrogenase Proteins 0.000 description 1
- 102000013009 Pyruvate Kinase Human genes 0.000 description 1
- 108020005115 Pyruvate Kinase Proteins 0.000 description 1
- 108010077895 Sarcosine Proteins 0.000 description 1
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 230000003292 diminished effect Effects 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 229940043257 glycylglycine Drugs 0.000 description 1
- 239000007999 glycylglycine buffer Substances 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 229930029653 phosphoenolpyruvate Natural products 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 229940075930 picrate Drugs 0.000 description 1
- OXNIZHLAWKMVMX-UHFFFAOYSA-M picrate anion Chemical compound [O-]C1=C([N+]([O-])=O)C=C([N+]([O-])=O)C=C1[N+]([O-])=O OXNIZHLAWKMVMX-UHFFFAOYSA-M 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 229940043230 sarcosine Drugs 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
Classifications
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- 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
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- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Organic Chemistry (AREA)
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- Physics & Mathematics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
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- Wood Science & Technology (AREA)
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- Bioinformatics & Cheminformatics (AREA)
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Abstract
СПОСОБ ОПРЕДЕЛЕНИЯ КРЕАТИНИНА В СЬгаОРОТКЕ КРОВИ, о т л ич а ю щ и и с тем, что, с целью повьшени специфичности способа, к пробе добавл ют гфеатининаминогвдролазу , инкубируют при рН 7,8-8,3 в течение 45-60 мин при 37°С и по уровню уменьшакщегос креатинина или образовавшегос креатина определ ют креатинин в пробе. i wMETHOD FOR DETERMINING CREATININ IN BLOOD TREATMENT, in a tl ia and so that, in order to increase the specificity of the method, hepatinin aminogram is added to the sample and incubated at pH 7.8-8.3 for 45-60 minutes at 37 ° C and creatinine in the sample is determined from the level of the decreased creatinine or the creatine produced. i w
Description
Изобретение относитс к медицине а именно к способу дл специфическ го ферметативного определени креатинина . Известе-н способ определени креа тинина путем смешивани креатинина с щелочным пикратом il . Однако данный способ вл етс недостаточно специфическим при вы в лении креатинина в сыворотке крови Цель изобретени - повышение специфичности способа. Поставленна цель достигаетс тем, что согласно способу определени креатинина к пробе добавл ют кр атининаминогидролазу, инкубируют при рН 7,8-8,3 в течение 45-60 мин при 37 С и по уровню уменьшающегос креатинина или образовавшегос креатинина определ ют креатинин в пробе. Способ осуществл ют следующим образом. Фермент - креатининаминогидролаз получают по известному методу. Этот фермент катализирует реакцию : Креатинамидогидролаза Креатинин+Н-рО у . : Креатин Образовавшийс креатин можно измерить известными способами, например , фосфорилированием креатиновой киназой и аденозинтрифосфатом (АТФ с образованием адёнозиндифосфата. Друга возможность состоит в измерении уменьшени количества креатинина по Жафе. Способ осуществл ют при рН между 7,8 и 8,3. Дл установки величины рН можно примен ть любые буферные растворы. Однако следует обращать внимание на то, чтобы примен емый буфер не преп тствовал используемом методу определени . Если, например затем по Жафе определ ют изменение содержани креатинина, нужно применить буфер, который не подавл ет реакцию Жафе. Неблагопри тные дл реакции, например, глициновые и гли цилглициновые буферные растворы. Предпочтительными вл ютс фосфатны и пирофосфатные буферы. Однако если определение производитс не по Жафе а образовавщийс креатин определ ют с помощью креатиновой киназы и АТФ . то можно примен ть также глициновые и им подобные буферные растворы. 9J Согласно предлагаемому способу предварительное отделение белка не требуетс . Однако отделение белка целесообразно дл последующего определени креатина. Креатин перевод т при применении фермента креатиназы в саркозин и мочевину и последнюю определ ют с помощью известных методов. Этот вид осуществлени способа примен етс дл определени фермента , содержащего креатинкиназу и креатиназу в смеси. Если образовавшийс креатин определ ют известным способом с применением креатиназы и АТФ, то отделение белка выгодно, так как благодар этому повышаетс чувствительность теста. Применение фермента, содержащего креатинамидогидролазу и креатиназу, предпочтительно, когда определение креатинина производитс по Жафе, так как благодар креатиназе равновесие перемещаетс в сторону образованн креатина. Изобретение создает также новую комбинацию реактивов дл специфического определени креатинина, котора состоит из креатинового стандарта , пикриновой кислоты, едкого натра, креатининамидогидролазы (одной или вместе с буфером), а также в том или ином случае креатиназы, в не смешиваемом до употреблени состо нии . Кроме того, комбинаци состоит из буфера, восстановленного никотинамид-аденин-динуклеотида (NADN), АТР и фосфоенолпирувата (ФЕП): лактатдегидрогенозы (LDH), пируваткиназы (РК) и MgC ; креатинкиназы (СК), креатининамидогидролазы в не смешиваемом до употреблени состо нии, 1 П р и м е р 1. Определение с непосредственно/ следующим применением реакции Жафе, 1,0 мл содержащей креатинин пробы (сыворотка или разбавленна моча) инкубируют в 0,050-0,2 М буфера (особенно пригодны пирофосфатный, фосфатный, диэтаноламии) HCR, или глицилглицин (НСЕ - буфер) креатининамидогидролазой в количестве минимум 5 и (тест), 1 U 1 ммоль, превращенного субстрата за 1 мин и креатиназой в количестве минимум 0,8 и (тест) при З7с в течение 453 60 мин. Затем производ т отделение белка с помощью 3 М трихлоруксусной кислоты вместе с пробой, к которой не прибавл ют смеси ферментов. В на досадочной жидкости обеих проб прово д т реакцию Жафе. Из разности экстинкций обеих проб при 546nm получаетс количество креатинина по отно шению к стандартной величине креатинина . Реакцию окрашивани по Жафе провод т путем добавлени пикриновой кислоты и NaOH, выдержки в течение 15 мин при комнатной температуре и измерени и кювете с толщиной сло 2 см при 546 . П р и м е р 2. Измерение креатина с помощью креатинкиназы. С помощью креатинкиназы креатинин гидролизуетс в креатин и образовавшийс креатин фосфорилируетс по известной методике креатинкиназой и АТФ. Образовавшийс АБФ превращаетс посредством ФЕК и ПК в АТФ и при этом получившийс пируват восстанавливаетс посредством NADH и лактатдегидрогеназы в лактат при 294 об1эазовании NAD. Обмен 1 ммоль NADH, измерение при 334, 340 или 366 п m (соответствует присутствию 1 ммоль креатинина). определени смесь реактивов, содержаща NADH, ATP, PEP и хлорид магни в 0,11 М буфера при рН 9,0 смешивают с лактатдегидрогеназой (LDH), пируваткиказой (РК) и термостатируют до . Затем добавл ют сыворотку и креатинкиназу, и при указанной температуре производ т инкубирование максимум в течение 30 мин. Путем добавлени минимум 5 U креатинкиназы начинают реакцию. Падение экстинкции регистрируют. Продолжительность реакции составл ет 40- 90 мин. Содержание креатина вычисл ют непосредственно по мол рным коэффициентам экстинкции NADH. Преимуществом данного способа вл етс повышение специфичности определени креатинина, упрощение по сравнению с базовым способом, отсутствие необходимости отделени белка в сыворотке крови.This invention relates to medicine, in particular to a method for the specific enzymatic determination of creatinine. The known method for the determination of creatinine by mixing creatinine with an alkaline picrate il. However, this method is not specific enough in the detection of serum creatinine. The purpose of the invention is to increase the specificity of the method. The goal is achieved by the method of determining creatinine by adding kr atininomine hydrolase to the sample, incubating at pH 7.8-8.3 for 45-60 minutes at 37 ° C and creatinine in the sample is determined by the level of diminished creatinine or creatinine. The method is carried out as follows. The enzyme creatinine aminogrolase is obtained by a known method. This enzyme catalyzes the reaction: Creatamide hydrolase Creatinine + H-pO y. : Creatine Creatine formed can be measured by known methods, for example, by phosphorylation of creatine kinase and adenosine triphosphate (ATP with the formation of adenosine diphosphate. Another possibility is to measure the decrease in creatinine Jafe. The method is performed at a pH between 7.8 and 8.3. To set the value Any buffer solution can be used in the pH. However, care should be taken that the buffer used does not interfere with the determination method used. If, for example, then the change in soda is determined by Jafe creatinine, a buffer that does not inhibit the Jafa reaction needs to be applied. Unsuitable for the reaction, for example, glycine and glycylglycine buffer solutions. Phosphate and pyrophosphate buffers are preferred. However, if the determination is not carried out by Jafe, the resulting creatine is determined by creatine kinase and ATP. glycine and the like buffer solutions can also be used. 9J According to the proposed method, no preliminary protein separation is required. However, protein separation is appropriate for the subsequent determination of creatine. Creatine is converted by the use of the enzyme creatinease to sarcosine and urea, and the latter is determined using known methods. This type of implementation of the method is used to determine an enzyme containing creatine kinase and creatinease in a mixture. If the creatine produced is determined by a known method using creatinease and ATP, the separation of the protein is beneficial, since it increases the sensitivity of the test. The use of an enzyme containing creatine, hydrolase and creatine, preferably, when creatinine is determined by Jafa, because, due to creatine, equilibrium is shifted towards creatine. The invention also creates a new combination of reagents for the specific definition of creatinine, which consists of a creatine standard, picric acid, caustic soda, creatinine dimethrolase (alone or with a buffer), and also in one or another case of creatinase, in a state that is not miscible before use. In addition, the combination consists of nicotinamide-adenine dinucleotide (NADN), ATP and phosphoenolpyruvate (PEP) buffer: lactate dehydrogenosis (LDH), pyruvate kinase (RK) and MgC; creatine kinase (CK), creatinamide hydrolase in a state that is not miscible before use, 1 EXAMPLE 1. Determination with Direct / Next Use of Gaefe reaction, 1.0 ml creatinine-containing sample (serum or diluted urine) is incubated at 0.050-0 , 2 M buffer (pyrophosphate, phosphate, diethanolamia) HCR, or glycylglycine (HCE - buffer) with creatinine amide hydrolase in an amount of at least 5 and (test), 1 U 1 mmol, converted substrate for 1 min and creatinase in at least 0.8 and (test) at 3-7s for 453 60 minutes. Then the protein is separated with 3 M trichloroacetic acid together with a sample, to which no enzyme mixture is added. In the annoying liquid of both samples, the reaction was performed by Jafa. From the difference in extinction of both samples at 546nm, the amount of creatinine is obtained relative to the standard value of creatinine. The Jacaf staining reaction is carried out by adding picric acid and NaOH, aging for 15 minutes at room temperature and measuring the cell with a layer thickness of 2 cm at 546. PRI mme R 2. Measurement of creatine with creatine kinase. With the aid of creatine kinase, creatinine is hydrolyzed to creatine and the resulting creatine is phosphorylated by the known method creatine kinase and ATP. The resulting ABP is converted by FEC and PC to ATP, and the resulting pyruvate is reduced by NADH and lactate dehydrogenase to lactate at 294 formation of NAD. Exchange 1 mmol NADH, measurement at 334, 340 or 366 p m (corresponds to the presence of 1 mmol creatinine). Determining a mixture of reagents containing NADH, ATP, PEP and magnesium chloride in 0.11 M buffer at pH 9.0 is mixed with lactate dehydrogenase (LDH), pyruvate case (RK) and thermostatically. Serum and creatine kinase are then added and incubation is carried out for a maximum of 30 minutes at the indicated temperature. By adding a minimum of 5 U, creatine kinase starts the reaction. Drop extinction register. The reaction time is 40 to 90 minutes. The creatine content is calculated directly from the molar extinction coefficients of NADH. The advantage of this method is to increase the specificity of the determination of creatinine, simplification compared with the basic method, no need to separate the protein in the blood serum.
Claims (1)
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 (1)
Publication Number | Publication Date |
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SU1144629A3 true SU1144629A3 (en) | 1985-03-07 |
Family
ID=5806955
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
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SU721777222A SU1144629A3 (en) | 1971-05-05 | 1972-04-17 | Method of determining creatinine in blood serum |
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
Non-Patent Citations (1)
Title |
---|
1. Биохимические методы исследовани в клинике. М., 1969, с. 103105. * |
Also Published As
Publication number | Publication date |
---|---|
DK139769B (en) | 1979-04-09 |
IT968190B (en) | 1974-03-20 |
FI53367B (en) | 1977-12-30 |
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 |
IL38918A (en) | 1974-12-31 |
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