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

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-IX 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. (C) 1998 Elsevier Science Ltd. All rights reserved.3671059106