Abstract
—(1) At least four distinct molecular forms of 4‐aminobutyrate: 2‐oxoglutarate aminotransferase from mouse and rat brain, have been separated by electrophoresis on paper, cellogel, agargel, silicagel and by immunoelectrophoresis.(2) The existence of specific typical electrophoretic profiles in mitochondrial and extramitochondrial compartments was shown.(3) A differential effect of pH on the anionic and cationic 4‐aminobutyrate:2‐oxoglutarate aminotransferase transaminase activities has been shown.(4) The possible consequences of the 4‐aminobutyrate: 2‐oxoglutarate aminotransferase isozyme compartimentation on the local availability of γ‐aminobutyric acid pools has been discussed.