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|Type:||Artigo de periódico|
|Title:||Purification And Characterization Of A Phosphodiesterase From Bothrops Alternatus Snake Venom|
|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.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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