SE407985B - PROCEDURE FOR PHOTOMETRIC ANALYSIS OF COAGULATION FACTORS - Google Patents
PROCEDURE FOR PHOTOMETRIC ANALYSIS OF COAGULATION FACTORSInfo
- Publication number
- SE407985B SE407985B SE7800304A SE7800304A SE407985B SE 407985 B SE407985 B SE 407985B SE 7800304 A SE7800304 A SE 7800304A SE 7800304 A SE7800304 A SE 7800304A SE 407985 B SE407985 B SE 407985B
- Authority
- SE
- Sweden
- Prior art keywords
- factor
- fibrin
- coagulation
- procedure
- coagulation factors
- Prior art date
Links
- 108010039209 Blood Coagulation Factors Proteins 0.000 title claims description 7
- 102000015081 Blood Coagulation Factors Human genes 0.000 title claims description 7
- 239000003114 blood coagulation factor Substances 0.000 title claims description 7
- 238000000034 method Methods 0.000 title claims description 4
- 238000005375 photometry Methods 0.000 title 1
- 108010073385 Fibrin Proteins 0.000 claims description 12
- 102000009123 Fibrin Human genes 0.000 claims description 11
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 claims description 11
- 229950003499 fibrin Drugs 0.000 claims description 11
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims description 9
- 239000004202 carbamide Substances 0.000 claims description 9
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 claims description 4
- 239000003795 chemical substances by application Substances 0.000 claims description 4
- 230000015271 coagulation Effects 0.000 claims description 4
- 238000005345 coagulation Methods 0.000 claims description 4
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 claims description 2
- 239000003593 chromogenic compound Substances 0.000 claims description 2
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 claims description 2
- 108010094028 Prothrombin Proteins 0.000 description 8
- 239000000758 substrate Substances 0.000 description 8
- 102100027378 Prothrombin Human genes 0.000 description 7
- 229940039716 prothrombin Drugs 0.000 description 7
- 239000003153 chemical reaction reagent Substances 0.000 description 5
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 4
- 108010054218 Factor VIII Proteins 0.000 description 4
- 102000001690 Factor VIII Human genes 0.000 description 4
- 108010074860 Factor Xa Proteins 0.000 description 4
- 108090000190 Thrombin Proteins 0.000 description 4
- 239000007983 Tris buffer Substances 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 229910001424 calcium ion Inorganic materials 0.000 description 4
- 229960000301 factor viii Drugs 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 229960004072 thrombin Drugs 0.000 description 4
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 238000010521 absorption reaction Methods 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 150000003904 phospholipids Chemical class 0.000 description 3
- 239000000523 sample Substances 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 108010048049 Factor IXa Proteins 0.000 description 2
- 108010014173 Factor X Proteins 0.000 description 2
- 230000008033 biological extinction Effects 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- TYMLOMAKGOJONV-UHFFFAOYSA-N 4-nitroaniline Chemical compound NC1=CC=C([N+]([O-])=O)C=C1 TYMLOMAKGOJONV-UHFFFAOYSA-N 0.000 description 1
- 102100022641 Coagulation factor IX Human genes 0.000 description 1
- 102100026735 Coagulation factor VIII Human genes 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108010029144 Factor IIa Proteins 0.000 description 1
- 108010076282 Factor IX Proteins 0.000 description 1
- 108010014172 Factor V Proteins 0.000 description 1
- 201000003542 Factor VIII deficiency Diseases 0.000 description 1
- 108010074864 Factor XI Proteins 0.000 description 1
- 108010080865 Factor XII Proteins 0.000 description 1
- 102000000429 Factor XII Human genes 0.000 description 1
- 208000009292 Hemophilia A Diseases 0.000 description 1
- 101000911390 Homo sapiens Coagulation factor VIII Proteins 0.000 description 1
- 108010000499 Thromboplastin Proteins 0.000 description 1
- 102000002262 Thromboplastin Human genes 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000003708 ampul Substances 0.000 description 1
- -1 benzyl-isoleucinyl-glutaminyl Chemical group 0.000 description 1
- 230000035602 clotting Effects 0.000 description 1
- 238000007820 coagulation assay Methods 0.000 description 1
- AGVAZMGAQJOSFJ-WZHZPDAFSA-M cobalt(2+);[(2r,3s,4r,5s)-5-(5,6-dimethylbenzimidazol-1-yl)-4-hydroxy-2-(hydroxymethyl)oxolan-3-yl] [(2r)-1-[3-[(1r,2r,3r,4z,7s,9z,12s,13s,14z,17s,18s,19r)-2,13,18-tris(2-amino-2-oxoethyl)-7,12,17-tris(3-amino-3-oxopropyl)-3,5,8,8,13,15,18,19-octamethyl-2 Chemical compound [Co+2].N#[C-].[N-]([C@@H]1[C@H](CC(N)=O)[C@@]2(C)CCC(=O)NC[C@@H](C)OP(O)(=O)O[C@H]3[C@H]([C@H](O[C@@H]3CO)N3C4=CC(C)=C(C)C=C4N=C3)O)\C2=C(C)/C([C@H](C\2(C)C)CCC(N)=O)=N/C/2=C\C([C@H]([C@@]/2(CC(N)=O)C)CCC(N)=O)=N\C\2=C(C)/C2=N[C@]1(C)[C@@](C)(CC(N)=O)[C@@H]2CCC(N)=O AGVAZMGAQJOSFJ-WZHZPDAFSA-M 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 230000006835 compression Effects 0.000 description 1
- 238000007906 compression Methods 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 229960004222 factor ix Drugs 0.000 description 1
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
- 208000009429 hemophilia B Diseases 0.000 description 1
- 238000003384 imaging method Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 125000001151 peptidyl group Chemical group 0.000 description 1
- 239000012488 sample solution Substances 0.000 description 1
- 238000002798 spectrophotometry method Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000012795 verification Methods 0.000 description 1
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/52—Use of compounds or compositions for colorimetric, spectrophotometric or fluorometric investigation, e.g. use of reagent paper and including single- and multilayer analytical elements
- G01N33/521—Single-layer analytical elements
- G01N33/523—Single-layer analytical elements the element being adapted for a specific analyte
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Hematology (AREA)
- Immunology (AREA)
- Engineering & Computer Science (AREA)
- Urology & Nephrology (AREA)
- Molecular Biology (AREA)
- Chemical & Material Sciences (AREA)
- Biomedical Technology (AREA)
- Food Science & Technology (AREA)
- Microbiology (AREA)
- Cell Biology (AREA)
- Biotechnology (AREA)
- Medicinal Chemistry (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Description
~ veoozoa-så 10 15 20 'I ._ met är faktor Vlla tillsammans med vävnadstromboplastín aktivatorn för faktor X. « 7 Av ritningen framgår att vid aktivering av faktor XII (sanno- likt genom kontakt med exempelvis kollagen) övergår denna till fak- tor XIIa, som påverkar faktor XI, som då övergår i aktiv form (Xla). ~ veoozoa-så 10 15 20 'IN ._ is factor Vlla together with the tissue thromboplastin activator for factor X. «7 The drawing shows that when activating factor XII (probable through contact with, for example, collagen), this is transferred to tor XIIa, which affects factor XI, which then turns into active form (Xla).
Faktorn Xla påverkar faktorn IX (antihämofili B-faktor) och denna Faktorn IXa tillsammans med kalciumjoner, fosfolipid och faktorn VIII (anti- hämofili A-faktor) påverkar faktor X, som aktiveras till faktor Xa.Factor Xla affects factor IX (anti-hemophilia B-factor) and this Factor IXa together with calcium ions, phospholipid and factor VIII (anti- hemophilia A factor) affects factor X, which is activated to factor Xa.
Denna faktor Xa påverkar faktorn II (protrombin) tillsammans med- övergår då i närvaro av kalciumjoner till faktorn IXa. kalciumjoner, fosfolipid och faktor Y, så att denna övergår i akti- verad form till faktor IIa (trombín), som i sin tur bringar fibrino- gen att övergå till fíbrin.This factor Xa affects factor II (prothrombin) together with then passes in the presence of calcium ions to the factor IXa. calcium ions, phospholipid and factor Y, so that it is converted into active formed into factor IIa (thrombin), which in turn causes fibrin gene to switch to fibrin.
Om nu en faktor saknas i blodet brytes hela reaktionsföljden - och fibrinbildning uteblir eller sker endast långsamt eller i ringa utsträckning.If a factor is now missing in the blood, the entire sequence of reactions is broken and fibrin formation is absent or occurs only slowly or in small amounts extent.
I de vanligaste koagulationsanalyserna använder man den tid som koagelbíldníngen fordrar som ett mått på aktiviteten av en el- ler flera av de faktorer, som deltar ü reaktionerna.In the most common coagulation assays, this time is used which the clot formation requires as a measure of the activity of an several of the factors involved in the reactions.
På senare tid har kromogena pepoidsubstrat i allt större om- fattning börjat användas för analys av koagulationsfaktorer i blod.Recently, chromogenic pepoid substrates have been increasingly compression has begun to be used for the analysis of coagulation factors in blood.
Efter aktivering av koagulationssystemet, vilket kan ske på olika sätt, kan man nu i många fall bestämma halten av en koagulations- faktor genom tillsättning av ett kromogent substrat, som är speci- fikt för faktorn ifråga, till ett blod- eller plasmaprov, i vilket koagulationskedjan har aktiverats. Den aktiverade koagulationsfak-_ torn har förmåga att digerera substratet, som i regel är en peptídyl- p-nitroanilid. Härvid frigöres p-nitfoanilin, som kan bestämmas spektrofotometriskt. ningen störande under den spektrofotometriska analysen.After activation of the coagulation system, which can occur in different way, one can now in many cases determine the content of a coagulation factor by the addition of a chromogenic substrate, which is fict for the factor in question, to a blood or plasma sample, in which the coagulation chain has been activated. The activated coagulation factor-_ tower is capable of digesting the substrate, which is usually a peptidyl p-nitroanilide. This releases p-nitophaniline, which can be determined spectrophotometric. disturbance during the spectrophotometric analysis.
Vid bestämningar av denna typ är fibrinbild-, Enligt föreliggande uppfinning undvikes angiven olägenhet.In determinations of this type, fibrin imaging, According to the present invention, the stated inconvenience is avoided.
Föreliggande förfarande kännetecknas av att till analyslösníngen sättes ett fíbrinlösande medel, som utgöres av karbamid eller en guanidin. Tillsatsen sker i något stadium under analysen ochi lämpligaste stadium kan man lätt fastställa genom för-försök för varje speciell analys. Medlet tillsättes i sådan mängd, att den ifrågavarande koagulationsfaktorns enzymatiska aktivitet väsent- ligen icke påverkas. . L Uppfinníngen beskrives närmare i följande exempel. 101 15 20 25 35 40 ' vandlas protrombin i plasma till trombin. 7800304-3 3 Exempel 1. Bestämning av halten protrombin i plasma En reagensblandning innehållande aktiverad faktor X (FXa), faktor V, fosfolipíd och kalciumjoner ("Ampoule P", IMCO, Stockholm) försättes med urea (karbamid) till en koncentration av 0,75 M. 1, 2 resp 5 pl plasma tillsättes till 1 ml av denna reagensblandning och den erhållna blandningen får stå vid 37°C under 2 min. 1 ml trisbuffert med pH 8,2 innehållande 0,75 M urea tillsättes jämte 0,2 ml 4 mM syntetiskt substrat, D-fenylalanyl-pipekolyl-L-arginin-p-nitroanílid ("S-2238", Kabi AB, Stockholm).' Av trombin frigjort p-nitroanilin bestämmes sedan spektrofotometriskt vid 405 nm. Ökningen i absorption per Härvid om- tidsenhet är direkt proportionell mot protrombinkoncentrationen i plasma (fig 1).The present method is characterized by the addition of the analysis solution a fibrin dissolving agent consisting of urea or a guanidine. The addition takes place at some stage during the analysis and most suitable stage can be easily determined by pre-experiment for each special analysis. The agent is added in such an amount that it the enzymatic activity of the coagulation factor in question not affected. . L The invention is described in more detail in the following examples. 101 15 20 25 35 40 'Prothrombin is converted in plasma to thrombin. 7800304-3 3 Example 1. Determination of plasma prothrombin content A reagent mixture containing activated factor X (FXa), factor V, phospholipid and calcium ions ("Ampoule P", IMCO, Stockholm) is added with urea (urea) to a concentration of 0.75 M. 1, 2 respectively 5 μl of plasma is added to 1 ml of this reagent mixture and the resulting mixture is allowed to stand at 37 ° C for 2 minutes. 1 ml Tris buffer with pH 8.2 containing 0.75 M urea is added along with 0.2 ml of 4 mM synthetically substrate, D-phenylalanyl-pipecolyl-L-arginine-p-nitroanilide ("S-2238", Kabi AB, Stockholm). ' Thrombin-released p-nitroaniline is determined then spectrophotometrically at 405 nm. The increase in absorption per In this case, unit of time is directly proportional to the prothrombin concentration in plasma (Fig. 1).
Exempel 2. Bestämning av faktor VIII i plasma _ Protrombin i ett plasmaprov aktiveras på känt sätt (se svenska patentskriften 7609456-4) och bildat trombin bestämmes med ett syn- tetiskt substrat.Example 2. Determination of factor VIII in plasma Prothrombin in a plasma sample is activated in a known manner (see Swedish 7609456-4) and the thrombin formed is determined by a thetic substrate.
(IMCO, Stockholm) försättes med 1, S resp 10 pl plasma. Provet in- kuberas i 120 s vid 37°C. Därefter tillsättes 1 ml trisbuffert innehållande 0,75 M urea och 0,2 ml 25 mM syntetiskt substrat, D-fenylalanyl-pipekolyl-L-arginin-p-nitroanilid ("S-2238", Kabi AB, Stockholm). i exempel 1. Denna ökning är korrelerad till plasmaprovets halt av faktor VIII.(IMCO, Stockholm) is added with 1, 5 and 10 μl of plasma, respectively. Tried in- incubate for 120 s at 37 ° C. Then 1 ml of Tris buffer is added containing 0.75 M urea and 0.2 ml 25 mM synthetic substrate, D-phenylalanyl-pipecolyl-L-arginine-p-nitroanilide ("S-2238", Kabi AB, Stockholm). in Example 1. This increase is correlated to the content of the plasma sample of factor VIII.
I båda de visade exemplen har trombinsubstrat använts. vis kan man även i exempel 2 använda ett substrat för faktor Xa, t ex bensyl-isoleucinyl-glutaminyl({-OR)-glutaminyl-arginin-p- nitroanilid (R = 50 % H; 50 % CH3) ("S-2222", Kabi AB, Stockholm). Även i detta fall är det viktigt att genom tillsats av urea hindra 150 pl av en reagensblandning för faktor VIII Ukningen av absorptionen bestämmes på samma sätt som uppkomsten av fibrintràdar i provlösníngen.In both the examples shown, thrombin substrates have been used. way, a substrate for factor Xa can also be used in Example 2, for example benzyl-isoleucinyl-glutaminyl ({- OR) -glutaminyl-arginine-p- nitroanilide (R = 50% H; 50% CH3) ("S-2222", Kabi AB, Stockholm). Even in this case, it is important to prevent the addition of urea 150 μl of a factor VIII reagent mixture The increase in absorption is determined in the same way as the appearance of fibrin threads in the sample solution.
Urea har vid försök visat sig lämpligast. Urea kan i beroende av den koagulationsfaktor som bestäms tillsättas i koncentrationer mellan 0,25 och 2 M. vering av vissa enzym.Urea has proved most suitable in experiments. Urea can be addicted of the coagulation factor determined is added in concentrations between 0.25 and 2 M. verification of certain enzymes.
Vid högre koncentrationer än 2 M sker inakti- Vid koncentrationer under 0,25 M kan fibrin- bildning ej fullständigt förhindras.At concentrations higher than 2 M inactivation occurs At concentrations below 0.25 M, fibrin formation is not completely prevented.
Exempel 3 a) 150 pl protrombinreagens (se exempel 1) försättes med 10 pl normal plasma. Efter en inkubationstid om 2 min tillsättes 1,0 ml 0,15 M trisbuffert med pH 8,2 och 200 pl 0,75 mM substrat, D-fenyl- alanyl-pipekolyl-L-arginin-p-nitroanilid ("S-2238", Kabi AB, Givet-' e 780030lf-3 4 Stockholm). Efter en ytterligare inkubatíonstid om 1 min avbrytes reaktionen med 150 pl ättíksyra och lösningens absorption bestämmes vid 405 nM. Extinktíonen är 0,300. Lösningen innehåller suspen- derat fibrín. b) Försöket enligt a) upprepas med den skillnaden, att protrombín- reagens som trisbuffert innehåller 0,1 M rešp 0,15 M guanidínium- hydroklorid. Extinktíonen blir i detta fall 0,240. Ingen fibrín- bildning har skett i detta fall. ---_-__----_---Example 3 a) 150 μl of prothrombin reagent (see Example 1) is added with 10 μl normal plasma. After an incubation period of 2 minutes, 1.0 ml is added 0.15 M Tris Buffer pH 8.2 and 200 μl 0.75 mM Substrate, D-Phenyl alanyl-pipecolyl-L-arginine-p-nitroanilide ("S-2238", Kabi AB, Given- ' e 780030lf-3 4 Stockholm). After an additional incubation period of 1 minute, discontinuation the reaction with 150 μl of acetic acid and the absorption of the solution is determined at 405 nM. The extinction is 0.300. The solution contains suspension derat fibrin. (b) The test referred to in (a) is repeated with the difference that prothrombin reagent as Tris buffer contains 0.1 M resp 0.15 M guanidinium hydrochloride. The extinction in this case becomes 0.240. No fibrin formation has taken place in this case. ---_-__ ---- _---
Claims (2)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SE7800304A SE407985B (en) | 1978-01-11 | 1978-01-11 | PROCEDURE FOR PHOTOMETRIC ANALYSIS OF COAGULATION FACTORS |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SE7800304A SE407985B (en) | 1978-01-11 | 1978-01-11 | PROCEDURE FOR PHOTOMETRIC ANALYSIS OF COAGULATION FACTORS |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| SE407985B true SE407985B (en) | 1979-04-30 |
Family
ID=20333640
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| SE7800304A SE407985B (en) | 1978-01-11 | 1978-01-11 | PROCEDURE FOR PHOTOMETRIC ANALYSIS OF COAGULATION FACTORS |
Country Status (1)
| Country | Link |
|---|---|
| SE (1) | SE407985B (en) |
-
1978
- 1978-01-11 SE SE7800304A patent/SE407985B/en unknown
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