Biochemical and functional characterization of a recombinant monomeric factor VIII-Fc fusion protein.

ABSTRACT:

Background

Hemophilia A results from a deficiency in factor VIII activity. Current treatment regimens require frequent dosing, owing to the short half-life of FVIII. A recombinant FVIII-Fc fusion protein (rFVIIIFc) was molecularly engineered to increase the half-life of FVIII, by 1.5-2-fold, in several preclinical animal models and humans.

Objective

To perform a biochemical and functional in vitro characterization of rFVIIIFc, with existing FVIII products as comparators.

Methods

 rFVIIIFc was examined by utilizing a series of structural and analytic assays, including mass spectrometry following lysyl endopeptidase or thrombin digestion. rFVIIIFc activity was determined in both one-stage clotting (activated partial thromboplastin time) and chromogenic activity assays,

SUBMITTER: Peters RT 

PROVIDER: S-EPMC3588154 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature