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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...
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