The purification and properties of 5-adenylic acid deaminase from muscle.

Schmidt (1) was the first to extract an enzyme catalyzing the deamination of 5-adenylic acid. He demonstrated the presence of adenosine and adenylic acid deaminases in NaHC03 extracts of saline-washed minced rabbit muscle. Purification of the preparation by adsorption with alumina removed the adenosine deaminase, thus demonstrating that deamination of adenylic acid and adenosine is catalyzed by two separate enzymes. Kalckar (2) was able to obtain active adenylic acid deaminase preparations by precipitating myosin by dialysis and subjecting the deaminase which remained in the supernatant fluid to ammonium sulfate fractionation between 0.3 and 0.5 saturation. In the present paper a method is described for the purification of deaminase, based on a combination of the procedures of Schmidt and Kalckar, and supplemented by the paper chromatographic technique for enzyme purification described by Mitchell et al. (3). Certain properties of the enzyme are described, particularly with respect to its interaction with stimulatory and inhibitory anions.