Differential digitonin extraction of rat liver mitochondria and of mitochondria of
livers of affected and unaffected male sparse fur mice released a lysine transcarbamylase activity
from the mitochondria at a digitonin to protein ratio in between that for myokinase and
glutamate dehydrogenase, but at a slightly lower ratio than the ornithine transcarbamylase
activity. Homocitrulline formation by isolated rat liver mitochondria is independent of the
uptake of lysine by mitochondria as evidenced by the insensitivity of homocitrulline formation
to changes in the matrix pH, in contrast to citrulline formation from ornithine. Highperformance
liquid chromatography separates the lysine transcarbamylase activity from the
ornithine transcarbamylase activity. It is concluded that the lysine transcarbamylase activity
is localized outside the inner mitochondrial membrane.
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