Abstract
Cytoplasmic tyrosine transaminase (L-tyrosine: 2-oxoglutarate aminotransferase, EC 2.6.1.5) was partially purified from normal, host liver and 3 Morris hepatomas and subsequently resolved by electrophoresis on polyacrylamide gels after hydrocortisone treatment. Enzyme activity was detected histochemically in situ on the gels. Seven enzymatically active forms were detected in normal liver. The presence of growing hepatomas altered the expression of this enzyme. Only 1, 2 and 4 activity peaks were detected in the host liver of animals with highly (most liver-like), well and poorly (least liver-like) differentiated hepatomas, respectively. Only 1, 4 and 6 peaks were detected, respectively, in highly, well and poorly differentiated hepatomas.