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Kinetic, Immunochemical, and Physical Studies on Purified Rat Liver Adenosine 5'-Phosphate Deaminase after Induction with 3'-Methyl-4-dimethylaminoazobenzene or Thioacetamide¹

Biomedical Division, The Samuel Roberts Noble Foundation, Inc., Ardmore, Oklahoma 73401

After induction with hepatocarcinogens and partial purification, kinetic, immunochemical, and physical properties of rat liver AMP deaminase were studied. The hepatic enzyme was induced by intraabdominal injections of thioacetamide or 3'-methyl-4-dimethylaminoazobenzene. Enzymes were purified by lithium sulfate precipitation, heat treatment, diethylaminoethyl cellulose chromatography, and gel filtration. The activity of both the induced enzyme and the normal enzyme was modulated by ATP, GTP, and alkali metal ions. Induction did not alter GTP inhibition of ATP activation. Data were obtained suggesting that citrate ion altered substrate affinity and inhibited ATP-GTP modulation of enzyme activity. Studies with antibody to rat liver AMP deaminase developed in rabbits indicated that the induced enzyme had essentially identical titration equivalence with the noninduced enzyme in both the crude and partially purified states. Lability of the induced enzyme cohort in the 105,000 x g supernatant fraction to heating at 55° was lost when it was partially purified.

¹ Portions of this work were financed by Grant DRG-1045 from the Damon Runyon Memorial Fund for Cancer Research, Inc., N. Y.

Received 11/23/70. Accepted 5/17/71.