Temperature-dependent ethanol inhibition of [14C]leucine incorporation in mouse heart slices.

: The incorporation of [C14]leucine into mouse heart slice proteins was temperature dependent, being maximal at 37 degrees C. Ethanol (200mM) produced an irreversible inactivation of the incorporation which was strongly temperature dependent, being only 8 percent at 34 degrees C, but 66 percent at 42.8 degrees C. The inactivation was proportional to the concentration. At 41.8 degrees C, even 40 mM ethanol produced a significant inhibition of incorporation. Ethanol affected the oxygen consumption of the slices much less than the [C14] leucine incorporation. Both acetone and dimethylsulfoxide produced similar, although less pronounced, effects. It is concluded that ethanol potentiates the heat inactivation of [C14] leucine incorporation into mouse heart slices due to its solvent effect.