Abstract
The large-amplitude swelling and phospholipase digestion techniques have been used to separate the outer- and the inner-membrane fractions of rat liver and brain mitochondria, and the distribution of monoamine oxidase (EC 1.4.3.4) in the fractions obtained has been compared with those of three other enzymes. The liquid nitrogen-temperature difference spectra of the reduced minus oxidized membrane fractions were also determined. The outer membrane fractions of liver mitochondria were rich in a cytochrome component with α-band maxima at 553 and 558 mμ but no evidence for such a cytochrome component in the outer membranes of brain mitochondria could be found. The results indicated that monoamine oxidase was at least partially located in the space between the outer and inner mitochondrial membranes. Penetration experiments showed that the inner of the two mitochondrial membranes was impermeable to a number of monoamine oxidase substrates.
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