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-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.
Smolka
M B
MB
Departamento de Bioquímica, Universidade Estadual de Campinas, SP, Brazil.
Marangoni
S
S
Oliveira
B
B
Novello
J C
JC
D000818:Animals; D017837:Bothrops; D003029:Coagulants / Q000302:isolation & purification*; D003435:Crotalid Venoms / Q000737:chemistry*; D005340:Fibrinogen / Q000737:chemistry; D008970:Molecular Weight; D013917:Thrombin / Q000302:isolation & purification*
D003029:Coagulants; D003435:Crotalid Venoms; D005340:Fibrinogen; D013917:Thrombin