Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194200
Type: Artigo de periódico
Title: Purification And Partial Characterization Of A Thrombin-like Enzyme, Balterobin, From The Venom Of Bothrops Alternatus.
Author: Smolka, M B
Marangoni, S
Oliveira, B
Novello, J C
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.
Subject: Animals
Bothrops
Coagulants
Crotalid Venoms
Fibrinogen
Molecular Weight
Thrombin
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/9690798
Date Issue: 1998
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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