Abstract
The purification of a phosphodiesterase from Bothrops atrox venom by chromatography on phosphocellulose and affinity chromatography with O‐(4‐nitrophenyl)‐O′‐phenyl‐thiophosphate ester coupled to activated Sepharose is described. Phosphatases are removed by chromatography on hydroxyapatite. The enzyme is a single‐chain protein with a molecular weight of approx 130000 as judged by dodecylsulfate‐gel electrophoresis and ultracentrifugation. It has a specific activity of 3.3 μmol bis(4‐nitrophenyl)phosphate hydrolyzed min−1 mg−1 at 24°C.
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