Is monoamine oxidase activity in the outer mitochondrial membrane influenced by the mitochondrial respiratory state?

Monoamine oxidase activity was measured in isolated rat liver mitochondria using the radiochemical assay with [14C]tyramine as substrate. With toluene as the extracting solvent the apparent activity in the resting state (State 4) was much higher than in the active state (State 3) in agreement with Smith and Reid (Smith, G.S. and Reid, R.A. (1978) Biochem. J. 176, 1011-1014). However, with ethyl acetate or diethyl ether as extracting solvents, the activity in both states was almost identical and several times higher than that measured with toluene. p-Hydroxyphenylacetaldehyde, p-hydroxyphenylacetalcohol and p-hydroxyphenylacetic acid were identified as final reaction products, the latter one being hardly extractable with toluene. It is concluded that monoamine oxidase activity is not influenced by the respiratory state of mitochondria and that differences found by Smith and Reid are due to different extractability of secondary reaction products. NADPH-dependent aldehyde reductase was tentatively identified in rat liver mitochondria, its specific activity amounting to about one fourth of that in the cytosol.