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In a recent paper we reported that monoamine oxidase (MAO) is localized on the outer membrane of rat liver mitochondria . We concluded that this enzymic activity could be used as a biochemical marker to monitor the physical separation of the outer membrane (OM), from the inner membrane plus matrix fraction (IMM), and from components housed between the membranes (6) . However, the use of MAO and rotenone-insensitive DPNH cytochrome c reductase (RIDCR) as markers for the outer membrane of rat liver mitochondria has been severely criticized by Green et al . (2) . In contrast to other workers, (1, 3-6) Green and co-workers assign enzymes of the citric acid cycle (except succinate dehydrogenase) and of fatty acid oxidation to sites on the outer membrane and MAO to the inner membrane . Green contends that, with regard to MAO localization, estimations of MAO are incorrect (a) due to errors in the spectrophotometric assay using benzylamine as substrate and (b) due to the high level of aldehyde dehydrogenase (ADH) in the mitochondria . The present paper should help to clarify this controversy as it specifically relates to the use of MAO as a marker for the OM of rat liver mito-

AN APPRAISAL OF THE USE OF MONOAMINE OXIDASE AS AN ENZYME MARKER FOR THE OUTER MEMBRANE OF RAT LIVER MITOCHONDRIA