title: Some characteristics of the Coagulation Factor Xa purified from human serum.
abstract: 1. Coagulation Factor X was purified from human serum to apparent homogeneity in disc gel electrophoresis, sodium dodecyl sulphate-polacrylamide-gel electrophoresis, immunoelectrophoresis and analytical ultracentrifugation. The method used was a modification of that described by Gladhaug & Prydz (1970). 2. The method permits the isolation of an activated form of Factor X (Xa) which has a molecular weight of about 25000. 3. Factor Xa is a glycoprotein containing about 14% carbohydrate. A preliminary report of the amino acid composition is given.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001797:Blood Protein Electrophoresis; D002241:Carbohydrates / Q000032:analysis; D004589:Electrophoresis, Disc; D004591:Electrophoresis, Polyacrylamide Gel; D005170:Factor X / Q000032:analysis / Q000302:isolation & purification*; D005643:Fucose / Q000032:analysis; D005690:Galactose / Q000032:analysis; D005947:Glucose / Q000032:analysis; D006023:Glycoproteins / Q000032:analysis; D006801:Humans; D007122:Immunoelectrophoresis; D008970:Molecular Weight; D012967:Sodium Dodecyl Sulfate; D014461:Ultracentrifugation
chemical_list: D000596:Amino Acids; D002241:Carbohydrates; D006023:Glycoproteins; D005643:Fucose; D012967:Sodium Dodecyl Sulfate; D005170:Factor X; D005947:Glucose; D005690:Galactose