Results 201 to 210 of about 145,714 (241)
Prevalence and Clinical Correlation of Intron 22 Inversion in Hemophilia A in Northeast India. [PDF]
CureusBarman R, Sarma A, Ahmed Z, Dutta A.
europepmc +1 more source
Acute Deep Vein Thrombosis Presents as an Early Complication of Wilson Disease. [PDF]
CureusFaroun A, Faroun R, Mashal R, Sultan M.
europepmc +1 more source
Effects of Protamine Reversal on Coagulation Parameters After High-Dose Heparin Administration in Percutaneous Hepatic Chemosaturation Intervention. [PDF]
Clin PractMetze M +9 more
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
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.
Ricardo H. Landaburu, Walter H. Seegers
openaire +3 more sources
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
openaire +3 more sources
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
openaire +3 more sources
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
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
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
openaire +3 more sources
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
openaire +3 more sources
[Rinsho ketsueki] The Japanese journal of clinical hematology, 2021
Dysprothrombinemia is the rarest inherited bleeding disorder that is characterized by a decrease in the prothrombin activity, but normal antigen levels. In this study, we report the case of a compound heterozygote of two mutations in prothrombin; Met337Thr and Arg388His, which has previously been identified as "Prothrombin Himi." A systemic blood ...
Yusuke Kamihara +7 more
openaire +2 more sources
Dysprothrombinemia is the rarest inherited bleeding disorder that is characterized by a decrease in the prothrombin activity, but normal antigen levels. In this study, we report the case of a compound heterozygote of two mutations in prothrombin; Met337Thr and Arg388His, which has previously been identified as "Prothrombin Himi." A systemic blood ...
Yusuke Kamihara +7 more
openaire +2 more sources
Decarboxylation of bovine prothrombin fragment 1 and prothrombin [PDF]
Biochemistry, 1979 Bovine prothrombin fragment 1 and prothrombin undergo decarboxylation of their gamma-carboxyglutamic acid residues when the lyophilized proteins are heated in vacuo at 110 degrees C for several hours. The fully decarboxylated fragment 1 product has lost its barium-binding ability as well as the calcium-binding function which causes fluorescence ...
Kenneth G. Mann +2 more
openaire +2 more sources