Preparation of Soluble Monoamine Oxidase

Since its discovery in 1928 monoamine oxidase has stubbornly resisted various attempts at purification. An explanation for this behavior emerged from the demonstration of the enzyme's intimate adherence to the cytoplasmic particulate elements. Various efforts were subsequently made to release this system into solution by means of disruption of these bodies. The result was either loss of activity or the production of smaller microscopic particles to which in turn the enzyme was attached. Such experiences strengthened the earlier opinion that "monoamine dehydrogenase" was a complex of several enzymes acting in unison or in sequence, in a fashion parallel to that postulated in the case of succinic dehydrogenase.