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Literature DB >> 4737324

A method for the simultaneous isolation of factor X and prothrombin from bovine plasma.

Abstract

1. A method is described for the simultaneous isolation of both Factor X and prothrombin from bovine plasma. The proteins are adsorbed on and eluted from barium sulphate and chromatographed on DEAE-Sephadex and are finally purified by rechromatography on DEAE-Sephadex. 2. The proteins can be purified in 48h from the collection of the blood and the method can be used to process large volumes of plasma. 3. The prothrombin has a molecular weight of 70300; the Factor X, on the other hand, is polydisperse, with most of the protein (86%) having a molecular weight of 56000.

Entities: Chemical Gene Species

Mesh：

Substances：
Prothrombin
Factor X

Year: 1973 PMID： 4737324 PMCID： PMC1177538 DOI： 10.1042/bj1310781

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

14 in total

1. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS.

Authors: B J DAVIS
Journal: Ann N Y Acad Sci Date: 1964-12-28 Impact factor: 5.691

2. A spectrophotometric determination of trypsin and chymotrypsin.

Authors: G W SCHWERT; Y TAKENAKA
Journal: Biochim Biophys Acta Date: 1955-04

3. The specific assay of Prower-Stuart factor and factor VII.

Authors: K W DENSON
Journal: Acta Haematol Date: 1961-02 Impact factor: 2.195

4. Preparation of highly purified prothrombin complex. I. Crystallization, biological activity, and molecular properties.

Authors: G H Tishkoff; L C Williams; D M Brown
Journal: J Biol Chem Date: 1968-08-10 Impact factor: 5.157

5. Exponential analysis of concentration or concentration difference data for discrete molecular weight distributions in sedimentation equilibrium.

Authors: R H Haschemeyer; W F Bowers
Journal: Biochemistry Date: 1970-01-20 Impact factor: 3.162

6. Purification and properties of bovine prothrombin.

Authors: J S Ingwall; H A Scheraga
Journal: Biochemistry Date: 1969-05 Impact factor: 3.162

7. Purification of a bovine plasma protein (factor VII) which is required for the activity of lung microsomes in blood coagulation.

Authors: W J Williams; D G Norris
Journal: J Biol Chem Date: 1966-04-25 Impact factor: 5.157

6. Membrane-dependent coagulation reaction is independent of the concentration of phospholipid-bound substrate: fluid phase factor X regulates the extrinsic system.

Authors: S D Forman; Y Nemerson
Journal: Proc Natl Acad Sci U S A Date: 1986-07 Impact factor: 11.205

6 in total

A method for the simultaneous isolation of factor X and prothrombin from bovine plasma.

1. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS.

2. A spectrophotometric determination of trypsin and chymotrypsin.

3. The specific assay of Prower-Stuart factor and factor VII.

4. Preparation of highly purified prothrombin complex. I. Crystallization, biological activity, and molecular properties.

5. Exponential analysis of concentration or concentration difference data for discrete molecular weight distributions in sedimentation equilibrium.

6. Purification and properties of bovine prothrombin.

7. Purification of a bovine plasma protein (factor VII) which is required for the activity of lung microsomes in blood coagulation.

8. Coagulant activity of tiger snake (Notechis scutatus scutatus) venom.

9. Studies on the formation of the prothrombin-converting complex.

10. The fractionation of Russell's-viper (Vipera russellii) venom with special reference to the coagulant protein.

1. An equilibrium study of metal ion binding to human plasma coagulation factor XIII.

2. The preparation of activated factor X and its action on prothrombin.

3. Turnover of factor X and of prothrombin in rabbits fed on a standard or cholesterol-supplemented diet.

4. Rapid purification of high purity thrombin and preparation of a novel hemostat for clinical purposes.

5. Association of tissue factor activity with the surface of cultured cells.

6. Membrane-dependent coagulation reaction is independent of the concentration of phospholipid-bound substrate: fluid phase factor X regulates the extrinsic system.