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

被引:33
作者
Smolka, MB [1 ]
Marangoni, S [1 ]
Oliveira, B [1 ]
Novello, JC [1 ]
机构
[1] Univ Estadual Campinas, Dept Bioquim, BR-13081970 Campinas, SP, Brazil
关键词
D O I
10.1016/S0041-0101(98)80008-1
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
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.
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收藏
页码:1059 / 1063
页数:5
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