The isolation and purification of a bovine-plasma protein which is a substrate for the coagulant fraction of Russell's-viper venom

Esnouf, M. P.; Williams, William J.

doi:10.1042/bj0840062

Cited by 174 publications

(60 citation statements)

References 8 publications

(3 reference statements)

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“…Under our conditions, DEAE Sephadex chromatography resulted in sepa ration of coagulation factor activity from many other plasma proteins, in- eluding albumin, y-globulin and fibrinogen. In accordance with other authors [13,18,34,45], a partial separation was effected between the factors II and X, the latter having a much higher affinity for the anion exchanger. The presence of DFP appeared to be necessary for prevention of acti vation of coagulation factors due to chromatographic procedures, as has been established by Jackson and Hanahan [17], Even in the presence of DFP, factor X eluted in a double peak as was observed previously by Jackson et al [18] and by M ilstone et al [31], We can confirm the finding of Jackson and Hanahan [17] that both kinds o f factor X have the same mobility on polyacrylamide electrophoresis.…”

Section: Discussionsupporting

confidence: 92%

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

Reekers¹,

Hemker²

1972

Pathophysiol Haemos Thromb

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The bovine coagulation factors II, VII, IX and X were separated from other plasma proteins, and each factor was obtained in a largely pure state by various chromatographic procedures in the presence of diisopropylfluorophosphate (DFP). Factor X was separated from factors II, VII, and IX by DEAE Sephadex chromatography, followed by G-100 filtration and hydroxylapatite chromatography. Separation of factors II and IX from factor VII was achieved by chromatography on DEAE cellulose, followed by G-100 gel filtration and hydroxylapatite chromatography. Factors II and IX were separated by preparative polyacrylamide electrophoresis. After DEAE cellulose chromatography, factor VII was purified by gradient elution from hydroxylapatite.

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Section: Discussionsupporting

confidence: 92%

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

Reekers¹,

Hemker²

1972

Pathophysiol Haemos Thromb

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“…This confirms results from this (9) and other laboratories (17,19). Macfarlane (17) and Williams and Esnouf (20,21) have demonstrated that calcium is necessary for the activation of Stuart factor by Russell's viper venom. We have found that the activation of proaccelerin by activated Stuart factor proceeds in the presence of citrate ions.…”

Section: Resultsmentioning

confidence: 99%

The Role of Proaccelerin in Human Blood Coagulation. Evidence that Proaccelerin Is Converted to a Prothrombin-converting Principle by Activated Stuart Factor: With Notes on the Anticoagulant Action of Soybean Trypsin Inhibitor, Protamine Sulfate, and Hexadimethrine Bromide*

Breckenridge

Ratnoff²

1965

J. Clin. Invest.

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“…Factor Xa was prepared from bovine serum as described by Esnouf and Williams (16). Conditions for the digestion of each preparation of the MBP-FX-PufQ fusion protein by factor X. were determined empirically.…”

mentioning

confidence: 99%

Recombinant expression of the pufQ gene of Rhodobacter capsulatus

et al. 1993

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Genetic studies have shown that the expression of the pufQ gene is required for normal levels of bacteriochlorophyll biosynthesis in Rhodobacter capsulatus. Yet, the exact function of the puJQ gene is unknown, and a puJQ gene product has never been isolated. We describe the recombinant overexpression of pufQ in Escherichia coli, as well as the purification and characterization of its gene product, the 74-amino-acid PufQ protein. Site-directed of R. capsulatus into operons and superoperons has recently been reviewed (37). The relative positions of the puf and puh operons and many of the bch and crt genes in the closely related bacterium Rhodobacter sphaeroides are similar to those found for the equivalent genes of R capsulatus (14). However, the distance between the puf and puh operons is some 10 kb shorter (40), and the photosynthetic gene cluster extends to include genes encoding other photosynthetic components, including cytochrome c2 (cycA) and the a-and 1-subunits of the B800-850 light-harvesting complex II (pucB and pucA, respectively, in the puc operon) (40).The biosynthesis of Bchl in both R. capsulatus and R.

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The isolation and purification of a bovine-plasma protein which is a substrate for the coagulant fraction of Russell's-viper venom

Cited by 174 publications

References 8 publications

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

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

The Role of Proaccelerin in Human Blood Coagulation. Evidence that Proaccelerin Is Converted to a Prothrombin-converting Principle by Activated Stuart Factor: With Notes on the Anticoagulant Action of Soybean Trypsin Inhibitor, Protamine Sulfate, and Hexadimethrine Bromide*

Recombinant expression of the pufQ gene of Rhodobacter capsulatus

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