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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Frischauf et al. (1973) studied this question.
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