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Aminooxyacetate is a potent inhibitor of glutamate: oxaloacetate transaminases from both rat and guinea pig kidney cortex. In guinea pig kidney cortex, phosphoenolpyruvate carboxykinase activity was found to be 59% cytoplasmic, 41% mitochondrial. Mitochondrial phosphoenolpyruvate carboxykinase activity is expressed only after sonication indicating that the enzyme is located within the inner mitochondrial membrane. Aminooxyacetate inhibits gluconeogenesis from lactate, but not from pyruvate, in both rat and guinea‐pig kidney cortex. It is concluded that gluconeogenesis in guinea‐pig kidney cortex proceeds by a pathway involving cytoplasmic, rather than mitochondrial phosphoenolpyruvate carboxykinase.
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Longshaw et al. (1972) studied this question.
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