Department of Pharmacology II, Osaka University School of Medicine, 3-57 Nakanoshima 4-chome, Kita-ku, Osaka 530, Japan
Abstract:
A putative precursor of rat liver mitochondrial glutamic oxaloacetic transaminase which was about 2,000 daltons larger than the subunits of the mature enzyme synthesized in vitro was sensitive to proteases (trypsin and chymotrypsin). When this precursor was incubated with isolated mitochondria in the absence of protein synthesis, it was processed to the mature form; the mature form co-sedimented with mitochondria and was resistant to externally added proteases. Mature enzyme did not compete with this transport.