Purification of the ADP-ribosylating enzyme from S-solfataricus by SDS-polyacrylamide gel electrophoresis and electroelution

The ADPribosylating enzyme from the thermophilic archaeon S. solfataricus w as purified by a simple procedure which included preparative electrophoresi s on a 0.1% SDS- polyacrylamide gel. The gel slice containing the enzymatic protein was cut Out and the enzyme was solubilized by electroelution. The pure enzyme was obtained by chromatography of the electroeluted sample on a DNA-Sepharose column. The purified enzyme retained both its full activity and the structuring ability as a function of temperature increase.