Abstract
Centrifugation of monoamine oxidase preparations from bovine liver mitochondria in sucrose gradients enabled the removal of most of the iron containing impurities without loss of catalytic activity. The nonheme iron content of the enzyme purified with a gradient was found to be not more than 5%, and the total iron not more than 25% of the flavin content of the enzyme. Thus, iron is not a component of monoamine oxidase. Most of the iron present was in the form of cytochrome impurities, the presence of which, in less pure preparations, obscured the observation of a red semiquinone formed on reduction of the enzyme with sodium dithionite. This semiquinone was not found on substrate reduction.
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