prothrombinase


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Related to prothrombinase: Stuart-Prower factor

prothrombinase

 [pro-throm´bin-ās]
2. the complex formed between activated factor x and calcium, phospholipid, and modified factor v; it can cleave and activate prothrombin to thrombin in the common pathway of coagulation. The term is sometimes used to refer specifically to the active enzyme center of the complex, which is activated factor x.

fac·tor X

in the clotting of blood, also known as: Stuart factor, Stuart-Prower factor, prothrombase, and prothrombinase. Its active form, factor Xa (EC 3.4.21.6), is formed from factor X by limited proteolysis and assists in the conversion of prothrombin to thrombin. A deficiency of factor X will lead to impaired blood coagulation.

prothrombinase

/pro·throm·bin·ase/ (-throm´bin-ās)
1. the complex of activated coagulation factor X and calcium, phospholipid, and modified factor V; it can cleave and activate prothrombin to thrombin.
2. sometimes specifically the active enzyme center of the complex, activated factor X.

prothrombinase

(prō-thrŏm′bə-nās′, -nāz′)
n.
An enzyme complex that catalyzes the hydrolysis of prothrombin to thrombin.

fac·tor X

(fak'tŏr)
A plasma coagulation factor that assists in the conversion of prothrombin to thrombin. Deficiency impairs blood coagulation.
Synonym(s): prothrombinase, Stuart factor, Stuart-Prower factor.

prothrombinase

; factor X blood enzyme that hydrolyses prothrombin, forming thrombin

fac·tor X

(fak'tŏr)
A plasma coagulation factor that assists in the conversion of prothrombin to thrombin.
Synonym(s): prothrombinase, Stuart factor, Stuart-Prower factor.

prothrombinase (prōthrom´binās),

n (complete thromboplastin, direct activator of prothrombin, extrinsic prothrombin activator), an inferred direct activator of prothrombin common to tissue and plasma coagulation systems. See also factor V.

prothrombinase

thromboplastin; tissue factor, factor III.
References in periodicals archive ?
Activated coagulation factor X (FXa) and activated factor V (FVa) assembled on a phospholipid surface comprise the prothrombinase complex that cleaves prothrombin to produce thrombin.
2+]-induced PS exposure and MV generation by evidence of increased thrombin generation based on the prothrombinase assay and thrombin generation in plasma (Figure 4A,B).
29)] Lupus Dabigatran or Not yet thoroughly anticoagulants rivaroxaban investigated (a) Methods based on the activation of coagulation at the prothrombinase level are unaffected [Lindahl et al.
Activated factor V (factor Va) is a cofactor protein in the prothrombinase complex that, together with the serine protease factor Xa, is responsible for conversion of prothrombin to the active enzyme thrombin.
Also known as factor X, prothrombinase is also a vitamin
labile factor) forms part of the prothrombinase complex, which
More recently, we reported that the variation in platelet GPVI content directly correlates with platelet prothrombinase activity, suggesting that platelet GPVI levels could represent yet another genetic risk factor for vascular thrombosis or excessive bleeding.
64) In addition, we found that prothrombinase activity induced by convulxin- or collagen-related peptide, but not ionophore A23187, is directly proportional to the platelet content of GPVI (P < .
Several recent studies showed that anti-CL/[beta]2-GPI/anti-PS/PT antibodies enhance the binding of [beta]2-GPI/PT to negatively charged PL in the prothrombinase reaction (35,45-48).
Assembly of the platelet prothrombinase complex is linked to vesiculation of the platelet plasma membrane: studies in Scott syndrome: an isolated defect in platelet procoagulant activity.
After its activation by thrombin and factor Xa, activated factor V (Va) forms an essential part of the prothrombinase complex, which catalyzes the conversion of prothrombin to thrombin in the presence of calcium and a phospholipid membrane (1).
PS also has a direct effect on the assembly of both tenase and prothrombinase complexes in purified systems (8-10), but the in vivo physiologic relevance of these biological activities remains to be demonstrated.