title: Purification and characterization of an abnormal factor IX (Christmas factor) molecule. Factor IX Chapel Hill.
abstract: Human Factor IX (Christmas factor) was isolated from the plasma of a patient with mild hemophilia B. The patient's plasma contained 5% Factor IX clotting activity but 100% Factor IX antigenic activity as determined by immunological assays, which included inhibitor neutralization and a radioimmunoassay for Factor IX. This abnormal Factor IX is called Factor IX Chapel Hill (Factor IXCH). Both normal Factor IX and Factor IXCH have tyrosine as the NH2-terminal amino acid. The two proteins have a similar molecular weight, a similar amino acid analysis, the same number of gamma-carboxyglutamic acid residues (10 gamma-carboxyglutamic acid residues), and a similar carbohydrate content. Both exist as a single-chain glycoprotein in plasma. The major difference between normal Factor IX and Factor IXCH is that the latter exhibits delayed activation to Factor IXa in the presence of Factor XIa and Ca2+. Thus, Factor IXCH differs from other previously described abnormal Factor IX molecules.
mesh_terms: D000328:Adult; D000595:Amino Acid Sequence; D002241:Carbohydrates / Q000032:analysis; D005164:Factor IX / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008297:Male; D008970:Molecular Weight; D009154:Mutation; D011498:Protein Precursors / Q000235:genetics
chemical_list: D002241:Carbohydrates; D011498:Protein Precursors; D005164:Factor IX