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see blood clottingblood clotting,
process by which the blood coagulates to form solid masses, or clots. In minor injuries, small oval bodies called platelets, or thrombocytes, tend to collect and form plugs in blood vessel openings.
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an enzyme of the hydrolase class, a major element in the blood-clotting system of man and animals. It is present in blood in the form of the inactive precursor prothrombin and is activated by prothrombinase, or active thromboplastin. Chemically, thrombin is a glycoprotein with a molecular weight of about 40,000; it contains about 5 percent carbohydrate.

Thrombin was isolated in crystalline form in 1972 by the American physiologist W. Seegers and his associates. It is similar in primary and tertiary structure to the serine proteolytic enzymes such as trypsin. A thrombin molecule consists of two polypeptide chains linked by a disulfide bond. The A chain of bovine thrombin contains 49 amino acid radicals, and the B chain, 265 radicals. The active center of the enzyme, as well as the carbohydrate constituent, are located in the B chain. Thrombin exists in several active forms, which differ in the structure of the B chain.

The main function of thrombin is to convert fibrinogen into fibrin. Thrombin hydrolyzes four arginyl-glycine bonds in the fibrinogen molecule. Four peptides then split off to form a fibrin monomer, which becomes polymerized into the fibrin clot that is the basis of a thrombus. The reactions of limited proteolysis with the participation of thrombin are accompanied by the activation of Factor XIII (fibrin stabilizing factor) and of Factors V and VIII, which take part in the reactions of the internal blood-clotting mechanism. Thrombin aids in platelet aggregation and in clot retraction. A relative excess of thrombin in the body has been shown to automatically initiate the activity of the anticoagu-lating system. This is accompanied by the introduction of heparin and the activator of plasminogen into the bloodstream, substances that help maintain the blood’s liquid state.

Thrombin is inactivated by diisopropyl fluorophosphate, which blocks the hydroxyl group of serine that enters the active center, and by other inhibitors characteristic of the serine proteinase group. Thrombin is inactivated in blood by the plasma antithrombins α2-macroglobulin, antithrombin III, and/or heparin. A specific nonplasma thrombin inhibitor is the polypeptide hirudin, found in the buccal glands of leeches.

Thrombin is used to arrest capillary bleeding by the application of fibrin foam soaked in thrombin to the affected surface.


Magnusson, S. “Thrombin and Prothrombin.” In The Enzymes, 3rd ed., vol. 3. New York–London, 1971.
“A New Thrombin: Purification, Aminoacid Composition, and Crystallization.” Thrombosis Research, 1972, vol. 1, p. 533.



An enzyme elaborated from prothrombin in shed blood which induces clotting by converting fibrinogen to fibrin.
References in periodicals archive ?
A total of 401 patients who had either active thrombosis or recent thrombotic episodes were tested for FVL and prothrombin G20210A mutations between January 1998 and September 1998.
The prevalence of Factor V Leiden and prothrombin G20210A mutations in an Albanian population Total n % Frequency FV 1691A 225 4 1.
The FV Arg506G1n and prothrombin G20210A mutations were identified as described previously (22).
To date, this concept has been tested in some groups known to have increased risk of thrombosis, such as women on oral contraceptives (79), patients with the prothrombin G20210A mutation (80), and patients treated with oral anticoagulants or heparin (81).
the prothrombin G20210A mutation and possibly the methylene tetrahydrofolate reductase (MTHFR) C677T mutation (24-26).

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