Abstract
Des-gamma-carboxy prothrombin (DCP), also known as protein induced by vitamin K antagonist (PIVKA-II), is a recognized clinical marker for hepatocellular carcinoma. Prothrombin contains 10 gluamic acid (Glu) residues within its N-terminus (GLA domain) which are post modified to gamma-carboxyglutamic acid (GLA). DCP is an abnormal form of prothrombin in which some of the 10 glutamic acid residues remain unmodified. A monoclonal antibody was developed to specifically recognize DCP, but not prothrombin. In this study we identified the epitope of the anti-DCP antibody using a series of short peptides representing the GLA domain. For each peptide, a single Glu residue was replaced with a GLA residue. The critical Glu residues recognized by the antibody were identified in a competitive format using fluorescence correlation spectroscopy (FCS). We also evaluated the DCP specificity of the antibody using homologues peptide from various GLA domain proteins present in various blood coagulation factors. The dissociation constant of the antibody was determined using FRET based method.
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