Properties of the monoamine oxidase of rat liver mitochondria.

摘要: Publisher Summary This chapter describes the progress of purification beef monoamine oxidase (MAO) and rat, rabbit, monkey liver MAO. The first major difference among these lies in manner solubilizing mitochondrial proteins. Earlier, a nonionic detergent was used for rat but this substance is not preferred because its nondiffusibility through cellophane membranes tendency to bind strongly In succeeding stage passage material, once fractionated with ammonium sulfate, redissolved, column Sephadex G-200 provides clear separation MAO from cytochrome c, which comes off rather later. partial achieved without loss activity. molecular weight MAO, determined by method gel filtration estimated be 290,000. It has been reported that purified preparation enzyme contains 0.12% 0.034% copper. Riboflavin deficiency renders hepatic more susceptible inhibition both vitro vivo. measuring fluorescence involves precipitation protein trichloroacetic acid. riboflavin causes distinct decrease activity, pyridoxine small increase. latter effect significant riboflavin-fed rats, does attain significance riboflavin-deficient animals.