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High-dose four-factor prothrombin complex concentrate for vitamin K antagonist reversal before urgent surgery: subanalysis of the LEX-209 randomized, active-controlled trial. [PDF]
Res Pract Thromb HaemostSarode R +6 more
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Prothrombin Synthesis in the Dog
American Journal of Physiology, 1964 Liver parenchymal cells were found to be the sites for production of prothrombin. Dogs were employed and their rate of prothrombin synthesis was modified as desired by giving either Coumadin or vitamin K1.
Marion Isabel Barnhart +2 more
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Haemostasis, 2009
Using recombinant DNA techniques, DNA fragments coding for bovine prothrombin mRNA have been cloned and characterized. Structural studies have revealed that prothrombin mRNA encodes a precursor protein having an amino-terminal extension of 43 amino acid residues.
R T, MacGillivray, D M, Irwin
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Using recombinant DNA techniques, DNA fragments coding for bovine prothrombin mRNA have been cloned and characterized. Structural studies have revealed that prothrombin mRNA encodes a precursor protein having an amino-terminal extension of 43 amino acid residues.
R T, MacGillivray, D M, Irwin
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Critical Reviews in Eukaryotic Gene Expression, 1998
Prothrombin and thrombin are involved in diverse biological functions. The structure of prothrombin has been studied extensively and its cDNA has been cloned from several species. The tissue-specific expression of this protein has been studied, as well as the developmental expression pattern.
S J, Degen, W Y, Sun
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Prothrombin and thrombin are involved in diverse biological functions. The structure of prothrombin has been studied extensively and its cDNA has been cloned from several species. The tissue-specific expression of this protein has been studied, as well as the developmental expression pattern.
S J, Degen, W Y, Sun
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Estimation of Prothrombin Level From Prothrombin Time
American Journal of Clinical Pathology, 1947Richard E Rosenfield
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THE ACETYLATION OF PROTHROMBIN
Canadian Journal of Biochemistry and Physiology, 1960Purified bovine prothrombin was acetylated to a range of 27 to 30% of its amino groups. Except for just significant amounts it lost its power to generate thrombin-C. Upon activation the yield of thrombin-E was 100% on the basis of the thrombin-C yield that was obtained on an aliquot sample of the prothrombin before acetylation.
R H, LANDABURU, W H, SEEGERS
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Electroimmunoassay of prothrombin
Thrombosis Research, 1987Electroimmunoassay of normal (10-Gla) and Gla-deficient prothrombins containing 0 to 9 Gla (gamma-carboxyglutamyl) residues performed in EDTA against anti- (normal) prothrombin showed that each of the Gla-deficient proteins contained as much antigenic activity as does the normal molecule. In the presence of Ca2+, however, normal prothrombin appeared to
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