Where does bovine thrombin come from?

THROMBIN-JMI, THROMBIN, Topical (Bovine), is a protein substance produced through a conversion reaction in which prothrombin of bovine origin is activated by tissue thromboplastin of bovine origin in the presence of calcium chloride. It is supplied as a sterile powder that has been freeze-dried in the final container.

What is bovine thrombin?

Product Description. Thrombin is an endolytic serine protease that selectively cleaves the Arg–Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B.

How to store thrombin?

Lyophilized Thrombin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thrmbin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).

How big is thrombin?

The molecular weight of prothrombin is approximately 72,000 Da. The catalytic domain is released from prothrombin fragment 1.2 to create the active enzyme thrombin, which has a molecular weight of 36,000 Da.

What is thrombin made from?

Thrombin is a naturally derived enzyme that is formed from prothrombin and acts as the basis for a fibrin clot by converting fibrinogen to fibrin. It is mainly used as a topical hemostatic agent in 5000- to 10,000-unit solutions, which accelerate capillary bleeding.

Where is thrombin synthesized?

the liver
Thrombin is synthesized in the liver and secreted into the general circulation in an inactive zymogen form (prothrombin), a complex multidomain glycoprotein that is activated to yield thrombin at sites of vascular injury by limited proteolysis following upstream activation of the coagulation cascade.

How do you dissolve thrombin?

The product is soluble in water (10 mg/mL), yielding a clear solution. Stock solutions can be prepared at a concentration of 100 units/mL in a 0.1% (w/v) BSA solution. Stock solutions remain active for one week at 0–5 °C. Solutions are most stable at pH 6.5, as a pH >7 will greatly reduce thrombin activity.

How do you make thrombin?

Thrombin can be prepared from blood plasma. The preparation involves three main steps: isolation of prothrombin from plasma, activation to thrombin, and purification of the mature enzyme from the activation mixture.

Is there thrombin in plasma?

The glycoprotein prothrombin, which occurs in blood plasma, is transformed into thrombin by a clotting factor known as factor X or prothrombinase; thrombin then acts to transform fibrinogen, also present in plasma, into fibrin, which, in combination with platelets from the blood, forms a blood clot.

What is the other name of thrombin?

Thrombin is available under the following different brand names: Recothrom, Thrombogen, and Thrombin JMI.

What converts prothrombin into thrombin?

prothrombinase
Prothrombin is transformed into thrombin by a clotting factor known as factor X or prothrombinase; thrombin then acts to transform fibrinogen, also present in plasma, into fibrin, which, in combination with platelets from the blood, forms a clot (a process called coagulation).

What is the NIH assay for thrombin concentration?

The NIH assay procedure uses 0.2 mL of diluted plasma (1:1 with saline) as a substrate and 0.1 mL of thrombin sample (stabilized in a 1% buffered albumin solution) based on a modification of the method of Biggs. Only clotting times in the range of 15-25 seconds are used for determining thrombin concentrations.

What is the concentration of prothrombin in normal human plasma?

The concentration of prothrombin in normal human plasma is 5–10 mg/dL. 3 Prothrombin is a glycoprotein with a glycan content of ~12%. 3

How is prothrombin cleaved in vivo?

Prothrombin is cleaved in vivo by activated factor X, releasing the activation peptide and cleaving thrombin into light and heavy chains yielding catalytically active α-thrombin. α-Thrombin is composed of a light chain (A chain, MW ~6 kDA) and a heavy chain (B chain, MW ~31 kDa).

What is the function of thrombin?

Thrombin is an endolytic serine protease that selectively cleaves the Arg–Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B. 1,2 The predominant form of thrombin in vivo is the zymogen, prothrombin (factor II), which is produced in the liver.