Abstract
Four hours after the administration of ethionine and in the face of an 80–90% depletion of hepatic ATP there is a twofold increase in cAMP. This increase in cAMP is shown not to be effected by a reduction in phosphodiesterase activity. Both the low K m and high K m forms of the enzyme retain their activity. The purification of liver plasma membranes is not affected by ethionine. There is a significant 20% increase in plasma membrane adenylate cyclase activity following acute ethionine intoxication. This was demonstrable using either ATP or 5′-adenylyl-imidodiphosphate as substrates. The plasma membranes, isolated in the presence of Ca 2+, have a 20-fold higher basal adenylate cyclase activity then previously reported and are not further stimulated by GTP or NaF. A modified protocol for isolating cAMP from the adenylate cyclase reaction is described.
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