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By V. Z. Gorkin

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This term is used to denote the apparent conversion of polyionic macromolecular aggregates (for example, mitochondria or their fragments) into an optically transparent homogeneous aqueous phase. Solubilization of amine oxidases implies their separation from membranes. An adequate method for solubilizing membrane-bound amine oxidases has to meet the following three main requirements: 1. The method has to ensure that most of the amine oxidase activity is extracted from the fraction sedimented after centrifugation (mitochon­ drial fraction) into the soluble protein fraction.

However, after fractionation of the mitochondrial suspension prepared from rat brain the monoamine oxidase activity (substrate tyramine) in the outer mitochondrial membrane constituted only 54% (but not 76% as was found in similar experiments with liver mitochondria) of the total monoamine oxidase activity occurring in both outer and inner mitochondrial membranes (Tipton, 1967). Moreover, using an electron microscope technique, monoamine oxidase activity (substrate tryptamine) has been detected in both outer and inner mitochondrial membranes of rat liver (Yoo and Oreland, 1976) and these findings were confirmed by estimations of monoamine oxidase activity (substrate benzylamine) (Turska and Turski, 1976).

3 Μ urea; insoluble particles were sedimented by centrifugation (60 min at 40,000 g) or 100,000 g) and discarded. Digitonin has been shown by electron microscopy to destroy the outer membrane of rat liver mitochondria (Schnaitman and coworkers, 1967). Micellar suspen­ sions (solutions) of digitonin were prepared by adding warm 0,25 Μ sucrose to recrystallized digitonin with sonication of the mixture 1-2 minutes later. The dispersions are transparent at 0°C for several hours (Erwin and Hellerman, 1967).

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