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pro vyhledávání: '"Jennifer P. DeAngelis"'
Publikováno v:
Thrombosis Research. 128:470-476
Introduction Activated protein C (APC) inactivates factor VIIIa (FVIIIa) through cleavages at Arg336 in the A1 subunit and Arg562 in the A2 subunit. Proteolysis at Arg336 occurs 25-fold faster than at Arg562. Replacing residues flanking Arg336 en blo
Publikováno v:
The Journal of biological chemistry. 287(19)
Factor (F)VIII can be activated to FVIIIa by FXa following cleavages at Arg(372), Arg(740), and Arg(1689). FXa also cleaves FVIII/FVIIIa at Arg(336) and Arg(562) resulting in inactivation of the cofactor. These inactivating cleavages occur on a slowe
Publikováno v:
Blood. 112(7)
Factor VIII consists of a heavy chain (A1A2B domains) and light chain (A3C1C2 domains), whereas the contiguous A1A2 domains are separate subunits in the cofactor, factor VIIIa. The intrinsic instability of the cofactor results from weak affinity inte
The cDNA encoding the luciferase from the Italian firefly Luciola italica was cloned using reverse transcriptase-PCR and a gene-specific primer set based on the DNA sequence of Luciola mingrelica. The cDNA sequence of L. italica luciferase was determ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff20b5f57e813aa08cc1ec8221e6bdc2
http://hdl.handle.net/11585/38604
http://hdl.handle.net/11585/38604
Publikováno v:
Blood. 110:2689-2689
Activated Protein C (APC) is an anticoagulant serine protease that proteolytically inactivates the coagulation cofactors, factors (F) Va and VIIIa. FVIIIa is a non-covalent heterotrimer consisting of A1, A2 and A3-C1-C2 subunits. APC-catalyzed inacti