Alcohol dehydrogenase capable of utilizing primary alcohols (straight and branched chain, unsaturated and cellosolves), secondary alcohols, polyhydric alcohols but not tertiary alcohols is described in the rat brain, lung, heart, liver, kidney, gut, spleen, pancreas, uterus, and seminal vesicle. With the straight chain primary alcohols the extent to which the alcohols were used increased relative to increasing chain length until the optimum length of six to seven carbon atoms had been reached, whereafter activity decreased, probably due to the insolubility of the higher members of the series in water. Side groups on the chain, double bonds and ethereal oxygen atoms, all had the effect of hindering the ease of dehydrogenation of the alcohol. Secondary alcohols were suitable as substrates; however, tertiary alcohols did not seem to be satisfactory for the demonstration of alcohol dehydrogenase. Polyhydric alcohols were suitable substrates although they were not as well used as were the monohydric alcohols. Furfuryl alcohol dehydrogenase was found in all tissues and is apparently a separate enzyme.