A kinetic evaluation of monoamine oxidase activity in rat liver mitochondrial outer membranes.
نویسندگان
چکیده
1. A preparation of mitochondrial outer membranes from rat liver can be shown to contain two kinetically distinct monoamine oxidase activities. These activities are distinguishable by their different sensitivities to the irreversible inhibitor clorgyline, and by the effect of the reversible inhibitors benzyl cyanide and 4-cyanophenol. 2. The substrate specificities of the preparation and the two enzyme species have been elucidated.
منابع مشابه
THE S U B M I T O C H O N D R I A L LOCALIZATION OF MONOAMINE OXIDASE An Enzymatic Marker for the Outer Membrane of Rat Liver Mitochondria
Controlled osmotic lysis (water-washing) of rat liver mitochondria results in a mixed population of small vesicles derived mainly from the outer mitochondrial membrane and of larger bodies containing a few cristae derived from the inner membrane. These elements have been separated on Ficoll and sucrose gradients. The small vesicles were rich in monoamine oxidase, and the large bodies were rich ...
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عنوان ژورنال:
- The Biochemical journal
دوره 139 3 شماره
صفحات -
تاریخ انتشار 1974