Abstract

There is a significant increase in hepatic cAMP binding activity 4 hr following ethionine intoxication. This activity is localized to the 100,000 g supernatant. The binding of cAMP by the 100,000 g supernatant of controls can be increased to experimental levels simply by dialysis. The increased binding activity seen during ethionine intoxication can be reversed by the administration of adenine. Neither S-adenosyl ethionine, S-adenosyl methionine, S-adenosyl homocysteine, nor AMP compete effectively with cAMP for the binding protein. Increasing ADP concentrations stimulates cAMP binding whereas increasing ATP concentration inhibits cAMP binding. At concentrations seen during ethione intoxication the effects of ADP and ATP were equal but opposite in direction.

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