Defibrinogenation with benzoyl-batroxobin.
The B. moojeni thrombic protease, batroxobin, was acylated by 4-amidinophenyl benzoate at the active site serine hydroxyl. From the enzymatically inactive benzoyl-batroxobin, batroxobin is generated with a half-life of deacylation of about one hour. The clotting activity of benzoyl-batroxobin in plasma is recovered with deacylation. The effects of batroxobin and benzoyl-batroxobin were studied following intravenous injection in rats. Compared to defibrinogenation with batroxobin, that obtained with benzoyl-batroxobin was much retarded. Batroxobin caused microthrombosis initially, which did not develop upon injection of benzoyl-batroxobin in equivalent doses.
D000215:Acylation; D012103:Batroxobin / Q000138:chemical synthesis / Q000378:metabolism*; D001665:Binding Sites; D001777:Blood Coagulation; D004546:Elapid Venoms; D005340:Fibrinogen / Q000378:metabolism*; D006207:Half-Life; D006801:Humans; D007700:Kinetics; D010447:Peptide Hydrolases / Q000378:metabolism*
D004546:Elapid Venoms; D005340:Fibrinogen; D010447:Peptide Hydrolases; D012103:Batroxobin