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Type: Artigo de periódico
Title: Purification and partial characterization of a thrombin-like enzyme, balterobin, from the venom of Bothrops alternatus
Author: Smolka, MB
Marangoni, S
Oliveira, B
Novello, JC
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-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.
Country: Inglaterra
Editor: Pergamon-elsevier Science Ltd
Citation: Toxicon. Pergamon-elsevier Science Ltd, v. 36, n. 7, n. 1059, n. 1063, 1998.
Rights: fechado
Identifier DOI: 10.1016/S0041-0101(98)80008-1
Date Issue: 1998
Appears in Collections:Unicamp - Artigos e Outros Documentos

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