The subunit structure of thrombin-activated factor V. Isolation of activated factor V, separation of subunits, and reconstitution of biological activity.

Esmon, Charles T.

doi:10.1016/s0021-9258(17)37898-5

Cited by 337 publications

(104 citation statements)

References 27 publications

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“…However, it should be mentioned that measurement of the inactivation rate without Ca*+ ions proved to be very difficult. Under these conditions factor Va looses its activity due to dissociation of the heavy and light chains (Esmon, 1979). Addition of APC to reaction mixtures without Ca*+ ions did, however, not result in acceleration of the spontaneous rate of factor Va inactivation.…”

Section: Resultsmentioning

confidence: 92%

“…In the 1960's the present name, factor V, was gradually adapted. Factor V has been purified to homogeneity from canine, bovine and human plasma (Nesheim e/ o/., 1979;Esmon 1979;Bolhuis ef a/., 1979;Dahlback, 1980;Kane and Majerus, 1981;Katzmann <?f o/., 1981;Suzuki e/ o/., 1982). The cDNA sequences for human , and recently, bovine factor V have been determined (Kane and Davie, 1986; Kane ef a/., 1987; Jenny e/ a/., 1987, Guinto <?/ a/., 1992) and from this the amino acid sequences could be deduced.…”

Section: Protein Cofactorsmentioning

confidence: 99%

“…Partially cleaved factor V already possesses full cofactor activity (Monkovic and Tracy, 1990). Fully thrombin activated factor V consists of a 105 kD heavy chain and a 71 and 74kD light chain doublet which are noncovalently associated through interactions that involve a single calcium ion (Ncsheim and Mann, 1979;Esmon, 1979;Guinto and Esmon, 1982). Russell's viper (K//?m/ rM.v.vt' ///' ) venom (RVV-V) activated factor V is cleaved between Arg'545 and Sei-1546 resulting in a large heavy chain and a light chain similar to the thrombin activated factor V (Suzuki ef a/., 1982;Dahlback, 1986; see Figure 2).…”

Section: T Tmentioning

confidence: 99%

“…Blood coagulation factor V is a single chain glycoprotein with a molecular weight of 330,000Da (Dahlbàck, 1980;Kane and Majerus, 1981) that contains three different types of protein domains (A, B and C) arranged in the order A1-A2-B-A3-C1-C2 (Jenny ef a/., 1987; Cripe e/ a/., 1992). Activation of human factor V by thrombin results in the removal of the major part of the B domain and the generation of factor Va, a molecule that consists of a heavy chain (containing the Al, A2 and a small piece of the B domain) and a light chain (containing the A3, Cl and C2 domains) that are associated via a single Cation (Esmon, 1979;Guinto and Esmon, 1982).…”

Section: Introductionmentioning

confidence: 99%

“…Factor V has little or no procoagulant activity (Nesheim e/ a/., 1979) and is converted into factor Va after proteolysis of specific peptide bonds which among others can be catalyzed by thrombin (Dahlbàck, 1980;Kane and Majerus, 1981;Suzuki e/a/., 1982). Thrombin-activated factor V is a twochain molecule (Suzuki e/ a/., 1982), that consists of a heavy chain and light chain held together by a tightly-bound calcium ion (Esmon, 1979;Guinto and Esmon, 1982). The heavy chainis derived from the amino-terminal region of factor V and has a MW of 105,000Da.…”

Section: Introductionmentioning

confidence: 99%

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Accelerin : the activated form(s) of human blood coagulation factor V

Bakker¹

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Section: Resultsmentioning

confidence: 92%

Section: Protein Cofactorsmentioning

confidence: 99%

Section: T Tmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Accelerin : the activated form(s) of human blood coagulation factor V

Bakker¹

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Blood Coagulation and Fibrinolysis

Colman

Budzynski

1985

Comprehensive Physiology

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The sections in this article are: Congenital Deficiencies in Initiation of Blood Coagulation Factor XII Plasma Prekallikrein Plasma Kininogens Interaction of Contact‐System Proteins Factor XI Factor IX Factor VIII Relationship of Intrinsic and Extrinsic Blood Coagulation Factor X Factor VII Thromboplastin Regulation of Prothrombin Activation Prothrombin Factor V Coagulant Phospholipid Surfaces Calcium Ions Thrombin Formation Thrombin Specificity Regulation of Thrombin Activity Heparin and Antithrombin III Interaction of Thrombin With Fibrin Nonmammalian Inhibitors of Thrombin Thrombinlike Enzymes in Snake Venoms Electron Microscopy of Fibrinogen Fibrinogen Structure Model of Fibrinogen Molecule Conversion of Fibrinogen to Fibrin Clot Polymerization Sites Cross‐Linking of Fibrin Interaction of Fibrinogen with Plasma Proteins Interaction of Fibrinogen with Cells Degradation by Proteases other than Plasmin Degradation of Fibrinogen and Fibrin by Plasmin Role of Fibrin in Clot Formation and Lysis Plasminogen and Plasmin Plasminogen Activators Inhibitors of Plasminogen and Plasmin Physiological Fibrinolysis

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