Abstract
In previous report one of the authors has reported that glutamic・pyruvic transaminase located at mitochondria has quite different natures from one in soluble fraction. We have isolated glutamic-oxalacetic transaminase from pig liver mitochondria (GOTM) about 20 times active more than original mitochondria suspension using the technique of ammonium sulfate fractionation, calcium phosphate gel absorption and zone electrophoresis. On calcium phosphate gel column, GOTM is eluted with 0.1M phosphate buffer at pH 8.0 and GOT in soluble fraction (GOTS) with 0.04M phosphate buffer at pH 7.0. On starch zone electrophoresis, they showed very contrary pattern, i. e., GOTM moved to cathode and GOTS to anode. GOTM was more labile than GOTS at 70℃ heating. In detecting optimum pH and temperature, was not found any remarkable difference. Thus the presence of two different type of GOT in different cell fraction was demonstrated. We are now undergoing the efforts to elucidate the significance of their localization from the view point of respiratory regulation and protein synthesis.
