Ribosome profiling of HEK293T cells overexpressing codon optimized coagulation factor IX
نویسندگان
چکیده
منابع مشابه
P-22: Codon Optimization of Coagulation Factor IX and Cloning in to The Chinese Hamster Ovary Cells
Background Human coagulation factor IX is a 57kDa plasma serine protease made in Liver which plays a vital role in the blood coagulation cascade. FIX deficiency causes severe disorder Hemophilia B or Christmas disease. Nowadays, recombinant proteins have important roles in treatment of diseases. Although, cultivated mammalian cells because of their ability for producing properly folded protein ...
متن کاملCoagulation Factor IX for Hemophilia B Therapy
Factor IX is a zymogen enzyme of the blood coagulation cascade. Inherited absence or deficit of the IX functional factor causes bleeding disorder hemophilia B, which requires constant protein replacement therapy. Reviewed herein are the current state in the manufacturing of FIX, improved variants of the recombinant protein for therapy, transgenic organisms for obtaining FIX, and the advances in...
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Eukaryotic translation initiation factors (eIFs) function at multiple steps. They enable the small 40S ribosome subunit to bind to initiator tRNA and mRNA, and scan to and select an initiation codon on the mRNA. They facilitate joining of the large 60S ribosome subunit, at which point the initiation phase of translation ends with the initiator tRNA in the P (peptidyl) site, and the ribosome poi...
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Previous studies have shown that thrombin generation in vivo caused a 92% decrease in factor IX (F.IX) activity and the appearance of a cleavage product after immunoblotting that comigrated with activated F.IX (F.IXa). Under these conditions, the fibrinolytic system was clearly activated, suggesting plasmin may have altered F.IX. Thus, the effect(s) of plasmin on human F.IX was determined in vi...
متن کاملProteolytic inactivation of blood coagulation factor IX by thrombin.
Coagulation factor IX is a vitamin K-dependent glycoprotein that circulates in blood as a precursor of a serine protease. Incubation of human factor IX with human alpha-thrombin resulted in a time and enzyme concentration-dependent cleavage of factor IX yielding a molecule composed of a heavy chain (mol wt 50,000) and a doublet light chain (mol wt 10,000). The proteolysis of factor IX by thromb...
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ژورنال
عنوان ژورنال: F1000Research
سال: 2020
ISSN: 2046-1402
DOI: 10.12688/f1000research.22400.1