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Transjugular Liver Biopsy for Histological Diagnosis of Refractory Ascites and Evaluation of Portal Hypertension. [PDF]

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Ishikawa T   +8 more
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Establishing altitude-based coagulation reference ranges in Western Sichuan. [PDF]

open access: yesSci Rep
Yuan Q   +10 more
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THE ACETYLATION OF PROTHROMBIN

Canadian Journal of Biochemistry and Physiology, 1960
Purified 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.
Ricardo H. Landaburu, Walter H. Seegers
openaire   +3 more sources

Activation of Prothrombin

American Journal of Physiology-Legacy Content, 1958
In experiments with purified biothrombin, it was found that strong solutions of sodium citrate or protamine sulfate (0.1% w/v) or purified platelet factor 3 depress the esterase activity and leave the clotting power unaltered. Apparently a depression of esterase activity is beneficial for the autocatalytic activation of purified prothrombin.
Walter H. Seegers, Ricardo H. Landaburu
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The Prothrombin Gene

Pathophysiology of Haemostasis and Thrombosis, 1986
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.
Ross T. A. MacGillivray, David M. Irwin
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The Biology of Prothrombin

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.
William Sun, Sandra J. Friezner Degen
openaire   +3 more sources

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