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Phenylalanine hydroxylase from human kidney
Enzyme
|January 1, 1975
Summary
Human kidney cortex contains phenylalanine hydroxylase (PAH) activity, offering a potential source for studying phenylketonuria. This enzyme is significantly less active in kidneys than in liver tissue.
Area of Science:
- Biochemistry
- Human Physiology
Background:
- Phenylalanine hydroxylase (PAH) is crucial for metabolizing phenylalanine.
- Understanding PAH distribution is vital for metabolic disorder research.
Purpose of the Study:
- To determine the presence and activity level of PAH in human kidney cortex.
- To compare kidney PAH activity with liver PAH activity.
- To assess the viability of kidney tissue as a source for PAH studies.
Main Methods:
- Enzyme activity assays were performed on surgically removed human kidneys.
- PAH activity was measured in human liver biopsies and autopsy samples for comparison.
- Autopsy tissues were analyzed to investigate postmortem enzyme stability.
Main Results:
- Phenylalanine hydroxylase activity was detected in human kidney cortex (average 47.2 mU/g).
- Kidney PAH activity was substantially lower than in human liver biopsies (average 217 mU/g).
- Autopsy liver and kidney samples showed minimal to no detectable PAH activity.
Conclusions:
- Surgically removed human kidneys contain active phenylalanine hydroxylase.
- Kidney tissue represents a viable alternative source for studying PAH and phenylketonuria.
- Postmortem degradation significantly impacts PAH activity in liver and kidney tissues.