In this report the presence,
and level, of phenylalanine hydroxylase in
the cortex of human kidney is established.
The average activity found in 15 surgically
removed kidneys was 47.2 ± 11.2 mU/g wet
weight of tissue. The average value, determined
under the same experimental conditions, for two human liver biopsies was 217 mU/g
tissue. Of five autopsy livers obtained 2.5-4 h postmortem, four contained no activity,
and only 1-2% of normal was found in the fifth. Autopsy kidneys were similarly inactive.
The presence of a highly active degradative enzyme could not be demonstrated in autopsy
liver homogenates; it was established that the lack of activity was not due to an inhibitory
component. A possible interpretation of this phenomenon is discussed.
According to work published elsewhere [3] the kidney and liver enzymes appear to be
similar. Thus, surgically removed kidneys provide an alternative source of human phenylalanine
hydroxylase which can be used to study phenylketonuria.
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