9002-04-4 Usage
Description
Thrombin is a trypsin-like serine protease enzyme that plays a crucial role in the clotting cascade of the human body. It is synthesized from prothrombin, a vitamin K-dependent zymogen, and is the last enzyme in the clotting cascade responsible for cleaving fibrinogen into fibrin, which forms the fibrin gel of a hemostatic plug or a pathologic thrombus.
Uses
Used in Coagulation Research:
Thrombin is used as a research tool for studying the coagulation process, protein-structure analysis, and biochemical research. It aids in understanding the mechanisms of blood clotting and platelet stimulation.
Used in Medical Research:
Thrombin is employed in medical research to investigate its potential applications in various medical conditions and treatments.
Used in Pharmaceutical Industry:
Thrombin is used in the development of pharmaceutical products, such as Thrombostat (Parke-Davis), which is a topical hemostatic agent.
Used in Tissue Repair:
Thrombin is used as a topical hemostatic agent for stopping local bleeding. It is synthesized from cow plasma and is applied topically to wounds to stop light bleeding from open vessels when other methods are not possible.
Used in Combination with Gelatin Sponge or Fibrin Foam:
Thrombin may initiate clotting when combined with gelatin sponge or fibrin foam, providing an effective hemostatic solution for various medical procedures.
For external use, thrombin is applied topically to the wound, as a solution containing 100 to 2,000 National Institutes of Health (NIH) units/mL in sodium chloride irrigation or sterile water for injection, or as a dry powder.
Biochem/physiol Actions
The main function of thrombin is the cleavage of fibrinogen to fibrin, to assist stable clot formation. A wide range of mutations in the prothrombin gene contributes to its deficiency resulting in coagulation disorders like dysprothrombinemia and hypoprothrombinemia. High levels of thrombin elicit neurotoxicity in dopaminergic neurons and contributes to the progression of Parkinson′s disease. Altered thrombin levels modulates the coagulation pathway in multiple sclerosis. Patients with coronary artery disease (CAD) show elevated levels of thrombin. Thrombin accumulation in neurofibrillary tangles of the brain may contribute to the aggregation of tau protein and pathophysiology of Alzheimer disease.
Purification Methods
Thrombin is purified by chromatography on a DEAE-cellulose column, while eluting with 0.1M NaCl, pH 7.0, followed by chromatography on Sephadex G-200. The final preparation is free from plasminogen and plasmin. [Yin & Wessler J Biol Chem 243 112 1968.] Thrombin from bovine blood is also purified by chromatography using p-chlorobenzylamino--aminocaproyl agarose, and gel filtration through Sephadex G-25. [Thompson & Davie Biochim Biophys Acta 250 210 1971.] Thrombin from various species was purified initially by precipitation of impurities with rivanol. [Miller Nature 184 450 1959.] Tissue inhibitor of metalloproteins (TIMP, from human blood plasma), Mr ~30,000. These are purified by an [anti-human amniotic fluid-TIMP]-Sepharose immuno-affinity column and eluted with 50mM glycine/HCl pH 3.0 buffer that is 0.5M in NaCl, and followed by gel filtration [Cawston et al. Biochem J 238 677 1986].
Check Digit Verification of cas no
The CAS Registry Mumber 9002-04-4 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 9,0,0 and 2 respectively; the second part has 2 digits, 0 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 9002-04:
(6*9)+(5*0)+(4*0)+(3*2)+(2*0)+(1*4)=64
64 % 10 = 4
So 9002-04-4 is a valid CAS Registry Number.
