Abstract
Human and bovine antithrombin II/III have been isolated by a simple procedure essentially using only affinity chromatography on heparin-agarose and polyethylene glycol precipitation. An additional ammonium sulphate step removes polyethylene glycol and trace contaminants. The final preparation is homogeneous by SDS-, disc- and agar slide electrophoresis. End group analysis of human antithrombin II/III shows histidine as the N-terminal amino acid. The pure preparation showed both progressive antithrombin activity and heparin cofactor activity.