Purificação e caracterização da fosfodiesterase do veneno de Bothrops alternatus (urutu)

AUTOR(ES)

Amanda Abdalla Valerio

DATA DE PUBLICAÇÃO

2002

RESUMO

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. 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 Kmof 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.4.

ASSUNTO(S)

enzimas cobra venenosa - veneno veneno - purificação

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