An Improved Method for the Purification of Staphylococcal Nuclease

Abstract

Abstract Commercial staphylococcal nuclease (Foggi strain) containing small amounts of contaminating protein can be purified by chromatography on phosphorylated cellulose columns. The purified enzyme is free of acid and alkaline phosphatase activities. It is homogeneous by polyacrylamide gel electrophoresis, and antigenically pure by immunodiffusion. The E1 cm1% of the pure enzyme at neutral pH is 9.3 at 280 mµ and 9.7 at 277 mµ.