[Isolation and properties of cortisol inducible and cortisol non-inducible isoenzymes of rat liver tyrosine aminotransferase]

Abstract

Rat liver contains two groups of tyrosine aminotransferase (TAT) isoenzymes; during electrophoresis in agar gel one of the groups moves to the anode and the other--to the catode. Cortisol is shown to induce only the anode isoenzymes of TAT, which were isolated, purified and thoroughly analyzed. The inducible anode isoenzyme of TAT spearated from other proteins is more sensitive to the effect of proteases (trypsin and chymotrypsin) than the catode isoenzyme. Some kinetic parameters of the purified TAT isoenzymes were studied. Both isoenzymes have pH optimum around 7.5; their apparent Km values for tyrosine are also similar. However, the catode isoenzyme of TAT possesses a higher affinity for alpha-ketoglutarate than does the anode isoenzyme. Unlike the latter, the former isoenzyme may use oxaloacetate as an amino group acceptor. Pyridoxal phosphate is firmly bound to the catode isoenzyme and can be readily spearated from the anode isoenzyme during dyalisis. An increased sensitivity of the inducible isoenzyme to proteases is due not only to the possibility of coenzyme dissociation, but also to some specific properties of the apoenzyme. The results obtained support the assumption that a high sensitivity of the inducible isoenzymes to proteases provides for a removal of excessive amounts of the enzymes from the cells under cessation of hormonal induction, thus maintaining enzymatic homostasis in the cell.