SATURABLE ETHANOL BINDING IN RAT-LIVER MICROSOMES

The binding of ethanol to rat liver microsomes is shown to be saturabl e at clinically relevant ethanol concentrations, whereas this effect i s not observed in extracted microsomal phospholipids. Brief exposure o f the microsomes to heat abolishes saturable ethanol binding. Equilibr ium binding data analysis, although only approximate in this context, suggests the presence of at least two groups of specific sites: high c apacity sites with affinities near the pharmacological range and low c apacity sites at lesser levels. The results indicate that the specific ity of ethanol for tissue is considerably greater than previously reco gnized.