Purification and partial characterization of a thrombin-like enzyme, balterobin, from the venom of Bothrops alternatus

Abstract A thrombin-like enzyme, balterobin, was purified from the venom of Bothrops alternatus . The purification steps included Sephadex G-75, heparin–sepharose and reverse phase HPLC C-18 column. Balterobin showed an apparent molecular weight of 30 000 in non-reduced conditions and displays a specific coagulant activity of 32.8 NIH units/mg over bovine fibrinogen. It also exhibits arginine amidase activity on DL-BAPNA. Like thrombin-like enzymes from other snakes, balterobin possesses valine as N-terminal residue, and is inhibited by PMSF.