A simple procedure for the extraction and purification of monoamine oxidase from pig brain mitochondria is described. The enzyme purified in this way appears to be homogeneous by cellulose acetate electrophoresis and the molecular weight was estimated to be approximately 102,000 by gel‐filtration. The purified enzyme is inhibited by iproniazid, chelating agents and a sulphydryl reagent. The Km value for tyramine has been determined as has its Ki value for high substrate inhibition.
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