Isolation and characterization of bovine factor VII.
Factor VII (proconvertin) has been purified approximately 5 x 10(5)-fold from bovine plasma with an overall yield of 30%. The isolation procedure involves barium sulfate adsorption and elution, DEAE-Sephadex batchwise adsorption and elution, benzamidine-agarose column chromatography, heparin-agarose column chromatography, and preparative polyacrylamide gel disc electrophoresis. The final product was homogeneous when examined by gel electrophoresis in the presence of sodium dodecyl sulfate. A minimal molecular weight of 45,500 was determined by sedimentation equilibrium. The molecular weight estimated by sodium dodecyl sulfate gel electrophoresis was 54,000. Factor VII is composed of a single polypeptide chain possessing an amino-terminal sequence of Ala-Asn-Gly-Phe-Leu-. The amino acid and carbohydrate compositions of factor VII are also reported.
D000117:Acetylglucosamine / Q000032:analysis; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D005167:Factor VII / Q000032:analysis*; D006493:Heparin; D006601:Hexoses / Q000032:analysis; D008970:Molecular Weight; D012794:Sialic Acids / Q000032:analysis
D000596:Amino Acids; D006601:Hexoses; D012794:Sialic Acids; D005167:Factor VII; D006493:Heparin; D000117:Acetylglucosamine