Purification of Blood Coagulation Factors II, VII, IX and X from Bovine Citrated Plasma

Reekers, P.; Hemker, H.C.

doi:10.1159/000213734

Cited by 3 publications

(2 citation statements)

References 11 publications

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“…Normal bovine factors II, IX, and X used for the immunization of rabbits were purified according to the method of Reekers [16]. Common inorganic chemicals (reagent grade), barium sulfate, acrylamide, l/'fl'-methylene bisacrylamide and benzamidine hydrochloride were obtained from Merck, Darmstadt, G.F.R.…”

Section: Methodsmentioning

confidence: 99%

Purification and properties of the phenprocoumon-induced decarboxyfactor X from bovine plasma

Lindhout

Kop-Klaassen

Kop

et al. 1978

Biochimica et Biophysica Acta (BBA) - Protein Structure

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1. By a procedure involving adsorption to barium sulfate, chromatography on DEAE-Sephadex and QAE-Sephadex and preparative polyacrylamide gel electrophoresis, decarboxyfactor X was purified from plasma of phenprocoumon-treated cows. No contaminants could be detected in the final preparation by polyacrylamide gel electrophoresis and zone-electrophoresis. 2. The molecular weight of decarboxyfactor X, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis is approximately 55 000, which is equal to that of factor X. The protein consists of two polypeptide chains with molecular weights of 44 000 and 17 000. 3. Decarboxyfactor X has antigenic determinants in common with normal factor X. 4. The amino acid composition and aminoterminal amino acids of normal factor X and decarboxyfactor X are identical. 5. Less than one residue of gamma-carboxyglutamate could be detected per mole of decarboxyfactor X. 6. In the absence of Ca2+, normal factor X has a slightly higher electrophoretic mobility than decarboxyfactor X. In the presence of Ca2+ the mobility of factor X decreases considerably while the mobility of decarboxyfactor X remains unaltered.

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Section: Methodsmentioning

confidence: 99%

Purification and properties of the phenprocoumon-induced decarboxyfactor X from bovine plasma

Lindhout

Kop-Klaassen

Kop

et al. 1978

Biochimica et Biophysica Acta (BBA) - Protein Structure

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“…When only Factor X is desired, the lower limits in the amount of barium sulfate suffice for > 80% removal of the Factor X. Barium carbonate is also used with equal effectiveness with oxalate anticoagulated plasma [62,93]. Barium citrate or aluminum hydroxide gel may also be used as an adsorbant in isolating Factor X and the other vitamin K-dependent clotting factors from plasma, in which case the anticoagulant used in collecting the blood in sodium citrate [5,83]. After separation of the barium sulfate from the plasma by centrifugation or, occasionally, simply settling, the barium sulfate is washed, using low ionic strength solutions of sodium chloride, sodium citrate, or sodium acetate, to remove occluded and loosely bound proteins.…”

Section: Isolation and Purification Of Bovine Factor Xmentioning

confidence: 99%

The Chemistry and Enzymology of Bovine Factor X

Henriksen¹,

Jackson²

2008

Semin Thromb Hemost

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In the currently proposed schemes for blood coagulation [14,57,94], Factor X lies at the point of convergence of two distinguishable routes by which clotting is initiated. These two routes have been labeled the intrinsic and extrinsic coagulation pathways. Factor X exists in the plasma in an enzymatically inactive or zymogen form which, during coagulation, is activated to yield the proteolytic enzyme Factor Xa. Activation of Factor X via the intrinsic pathway requires only plasma-contained clotting factors, while the extrinsic pathway requires the participation of tissue-derived substances as well as plasma factors. The only known physiologic substrate for Factor Xa is another zymogen, prothrombin, which is activated to yield the protease thrombin. In turn, thrombin acts upon fibrinogen-yielding fibrin, which polymerizes to form a fibrin clot. Since the activation of Factor X is the first reaction common to both the intrinsic and extrinsic coagulation pathways, this activation process must be viewed as a key event in initiating thrombin formation as well as subsequent fibrin clot formation. Likewise, control of this activation process, as well as the consequent action of Factor Xa, becomes critical to regulating the formation and subsequent action of thrombin.A vitamin requirement for normal blood coagulation was first shown from the work of Dam [12], who named this vitamin "vitamin K." It was subsequently demonstrated that vitamin K was necessary for the formation of four specific plasma proteins, blood coagulation factors VII [52,77], IX [64,71,84], and X [3,42,84] in addition to prothrombin [89]. Of these proteins, in addition to Factor X itself, one is the substrate for Factor Xa, and the other two are responsible for Factor X activation.In the present discussion, we shall consider the isolation and characterization of Factor X, the process by which it is activated to yield Factor Xa, and finally the properties of Factor Xa as a proteolytic enzyme. This is not intended as a comprehensive review of all work in the field, but rather a presentation of what we believe to be salient features of Factor X chemistry and enzymology as well as recent developments in this field. The authors recognize that the development or our understanding of the chemistry and function of Factor X is the product of the contributions of many workers, some of whom may not be explicitly credited. We apologize for such omissions and would welcome their being called to our attention.

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A coagulation reagent completely devoid of factor X; Relation between clotting time and concentration of factor X

Vermeer

Soute

Hemker

1979

Thrombosis Research

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Purification of Blood Coagulation Factors II, VII, IX and X from Bovine Citrated Plasma

Cited by 3 publications

References 11 publications

Purification and properties of the phenprocoumon-induced decarboxyfactor X from bovine plasma

Purification and properties of the phenprocoumon-induced decarboxyfactor X from bovine plasma

The Chemistry and Enzymology of Bovine Factor X

A coagulation reagent completely devoid of factor X; Relation between clotting time and concentration of factor X

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