The chromatographic separation of phosphatases in snake venoms.

This report describes a method of preparing samples of phosphodiesterase suitable for some chemical studies of desoxyribonucleic acid. A study of the use of purified phosphodiesterase in hydrolyzing thymonucleic acid has already been made (1). The source of our phosphodiesterase (snake venoms) was suggested by the work of Gulland and Jackson (2), although it now seems to us that their conclusions were misleading. Since the venoms of some snakes would not hydrolyze monophenyl phosphate, they concluded that phosphomonoesterase was absent. In a subsequent paper (3), however, they showed that these same venoms would hydrolyze adenosineor inosine5-phosphate and named the enzyme responsible “5-nucleotidase.” Acting on the conclusion of Gulland and Jackson, we tested the action of “stypven”’ on magnesium oligonucleotide from thymonucleic arid. It liberated very little inorganic phosphate, while lyophilized Russell’s viper venom from another source2 did so very actively. A possible clue to this difference in activities was afforded by the statement of Burroughs Wellcome that their material had been subjected to a bacterial filtration. It seemed possible that phosphomonoesterase had been removed selectively by this procedure. The work described below arose out of our investigation of the result of filtration through a Seitz filter on solut,ions of lyophilized snake venoms.