The present study has examined the affinities of sheep plasma semicarbazide-sensitive amine oxidase (SSAO) enzymes for a range of aliphatic amines and also the effects of two inhibitory compounds, beta-aminopropionitrile (BAPN) and mexiletine. Two kinetically separable enzyme activities appeared to be responsible for the metabolism of amines containing 2-5 carbon atoms while the deamination of higher amines and methylamine and allylamine produced kinetic plots characteristic of only one enzyme activity. When benzylamine metabolism was used as an indication of enzyme activity, the two inhibitors had different effects. BAPN exhibited predominantly a mixed pattern of inhibition while the effects of low concentrations of mexiletine were largely competitive. These results present evidence confirming the presence of two kinetically separable SSAO activities in sheep plasma, although we must await the development of highly selective inhibitors before these two activities can be fully resolved.