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Blood Coagulation Factor Ix: Purification, Activation, Crystallization, Juliet Mcgill
Blood Coagulation Factor Ix: Purification, Activation, Crystallization, Juliet Mcgill
WWU Honors College Senior Projects
This paper presents readers with an optimized procedure for the purification, activation, and crystallization of selected blood coagulation Factor IX double mutant (FIX_2). Through the completion of this work, we aim to enhance future biochemical and structural studies by providing an easier means for the FIX_2 production, in order to increase understanding of the protein’s function within the blood coagulation cascade. The initiation of the blood coagulation cascade is brought on by activation of inactive Factor VIII (FVIII) protein though contact with tissue factor, the FVIII protein then binds to an activated platelet surface where it must wait for its …
Lipid Binding Studies Of Blood Coagulation Factor Viii C1 And C2 Domains, Rachel L. Blazevic
Lipid Binding Studies Of Blood Coagulation Factor Viii C1 And C2 Domains, Rachel L. Blazevic
WWU Honors College Senior Projects
Blood coagulation factor VIII (fVIII) is an essential cofactor in the mammalian blood-clotting cascade. fVIII must bind the phospholipid membrane of activated platelets to function as a cofactor for fIXa. The blood coagulation cascade culminates in the formation of a stable blood clot. In humans, the C1 and C2 domains are implicated in binding phospholipid membranes, however the relative contribution of different residues in the lipid-binding mechanism is unclear. Using site-directed mutagenesis, expression of the isolated C1 and C2 domains in Escherichia coli cells, protein purification with metal affinity chromatography, electrospray ionization mass spectrometry, enzyme-linked immunosorbent assays, liposome sedimentation assays, …