Electrophoretic migration pattern of serum glutamic oxalacetic transaminase.

THE ENZYME GLUTAMIC OXALACETIC ThANSAMINASE (GO-T), which serves as a catalyst for the reversible reaction of a-ketoglutarate and l-aspartate to produce oxalacetate and i-glutamate in biologic systems, has long been known to be a normal component of the serum proteins. The enzyme is widely distributed in animal and human tissues but its greatest activity has been found in homogenates of heart muscle, skeletal muscle, brain, liver, kidney, testis, lung, and spleen, in decreasing order (1, 2). In recent years, as a result of the development by Karmen (3) of a simplified, accurate, and fairly rapid method for the determination of the activity of the enzyme, considerable interest has been aroused in the clinical implications of increased levels of this enzyme in human and animal sera during certain pathologic states involving damage to these transaminase-rich tissues. The current work being reported in the literature deals primarily with attempts to correlate the elevated serum levels of GO-T with the extent of damage to these tissues.