Abstract
The existence of a specific mechanism for glutamine transport is demonstrated by observation that brain mitochondria swell when incubated in iso-osmolar solutions of this neutral amino acid. There is no proton or ionophore requirement, but a metabolic energy supply increases the rate of swelling. Carrier mediation is strongly suggested by the observation that l-glutamine is transported more rapidly than its d-isomer. Transport is inhibited by ionic mercurials, but not by N-ethylmaleimide, which rules out any link between glutamine uptake and glutamate efflux, α-ketoglutarate and glutamate are powerful inhibitors of glutamine transport. Interactions between the specific glutamine transport mechanism and the intramitochondrial phosphate-dependent glutaminase activity are discussed.
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