Ruscák M, Orlický J
Physiol Bohemoslov. 1975;24(6):543-9.
The authors describe different properties of brain mitochondrial and cell sap alanine aminotransferase. They showed that the mitochondrial enzyme was inhibited by maleate, chlorides, acetate and phosphate with a high ionic strength (over 1.8), that its pH optimum lay between 7.5 and 8.5, that it was thermolabile at over 40 degrees C and that it was salted out from solutions with ammonium sulphate at 0.6--0.8 saturation. The activity of the cell sap enzyme was inhibited by phosphate at an ionic strength of only 0.12, less markedly by maleate and not at all by chlorides and acetate; its pH optimum was about 8, it was thermostable up to 60 degrees C and was precipitated from ammonium sulphate solution at between 0.35 and 0.6 saturation. The authors conclude from their results that two different alanine aminotransferase enzymes are present in the CNS.
