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- W955707940 abstract "This chapter describes the progress of purification of beef monoamine oxidase (MAO) and of the rat, rabbit, and monkey liver MAO. The first major difference among these lies in the manner of solubilizing the mitochondrial proteins. Earlier, a nonionic detergent was used for rat but this substance is not preferred because of its nondiffusibility through cellophane membranes and its tendency to bind strongly to the proteins. In a succeeding stage of the purification the passage of the material, once fractionated with ammonium sulfate, and redissolved, through a column of Sephadex G-200 provides a clear separation of MAO from cytochrome c, which comes off the column rather later. This partial purification is achieved without loss of activity. The molecular weight of rat liver MAO, determined by the method of gel filtration is estimated to be 290,000. It has been reported that a purified preparation of the rat liver enzyme contains 0.12% and 0.034% copper. Riboflavin deficiency renders the hepatic MAO of the rat more susceptible to inhibition both in vitro and in vivo. The method of measuring the fluorescence in purified enzyme involves precipitation of the protein with trichloroacetic acid. The deficiency of riboflavin causes a distinct decrease in MAO activity, but pyridoxine deficiency causes a small increase. The latter effect is not significant in the riboflavin-fed rats, but does attain significance in riboflavin-deficient animals." @default.
- W955707940 created "2016-06-24" @default.
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- W955707940 date "1968-01-01" @default.
- W955707940 modified "2023-09-27" @default.
- W955707940 title "Properties of the Monoamine Oxidase of Rat Liver Mitochondria" @default.
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- W955707940 doi "https://doi.org/10.1016/s1054-3589(08)61156-4" @default.
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