Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/101814
Type: Artigo de periódico
Title: Purification And Characterization Of A Phosphodiesterase From Bothrops Alternatus Snake Venom
Author: Valerio A.A.
Corradini A.C.
Panunto P.C.
Mello S.M.
Hyslop S.
Abstract: A phosphodiesterase was purified from the venom of the snake Bothrops alternatus by a combination of gel filtration and ion exchange chromatographies. In SDS-PAGE, the enzyme gave a single band with a molecular mass of 105 kDa, which was unaltered in the presence of β-mercaptoethanol, indicating that the protein contained no subunits. A single protein band was also observed in native PAGE. There were no contaminating 5′-nucleotidase, alkaline phosphatase and protease activities. The enzyme was recognized by commercial bothropic antiserum and gave a single band in immunoblotting. The enzyme had a pH optimum in the range of 7.5-9.5 and the optimum temperature was 60°C, with activity being rapidly lost within 1 min at ≥70°C. The Km of the enzyme was 2.69 mM. PDE activity was potentiated by cobalt and, to a lesser extent, by calcium, whereas copper, manganese, zinc, EDTA, and β-mercaptoethanol were inhibitory. These properties show that this enzyme is very similar to that isolated from other snake venoms. © 2003 Plenum Publishing Corporation.
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Rights: fechado
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Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-52649171365&partnerID=40&md5=cb9ab5b775b70d90b6d53abbefe7fb7e
Date Issue: 2002
Appears in Collections:Unicamp - Artigos e Outros Documentos

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