Abstract
We measured hepatic alanine:glyoxylate aminotransferase (AGT) activity using capillary electrophoresis. After rat liver homogenate was incubated in the presence of substrates and pyridoxal 5′-phosphate, the pyruvate and glycine produced by AGT were measured. The AGT activity was 10.02±0.31 μmol pyruvate/h/mg protein and 10.21±0.15 μmol glycine/h/mg protein. This method is relatively simple and shows superior sensitivity, allowing the measurement of enzyme activity in 5 μg of protein. Therefore, it appears to be suitable for laboratory use and may also have advantages for measuring AGT activity in liver biopsy specimens.
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