Immunological evidence for existence of two subforms of soluble glutamic oxaloacetic transminase (sGOT) in human and rat brain.

Using a sensitive and specific antiserum, the existence of two subforms of soluble glutamic oxaloacetic transaminase in both rat and human brain has been demonstrated. In the rat, the two proteins each have a molecular mass of 47,000 daltons. The more abundant basic protein has an isoelectric point of 5.9 while the sparsely staining more acidic protein has an isoelectric point of 5.8. In the human the two proteins visualized each have a molecular mass of 43,000 daltons. The more abundant basic protein has an isoelectric point of 5.7 while the sparsely staining more acidic protein has an isoelectric point of 5.6. In both rat and human, it seems reasonable to conclude that the abundant basic protein that reacts with the antiserum is the ? subform of the enzyme, while the sparsely staining more acidic protein is the ? subform of the enzyme. These results are of interest for a number of reasons. First, they establish the existence of at least two subforms of soluble glutamic oxaloacetic transaminase in both rat and human brain. Secondly, they show that this enzyme is a major protein visible on two-dimension gels of rat and human brain and that this enzyme is widely distributed throughout the central nervous system. Finally, they positively identify two more proteins visible on two-dimension gels generated using rat or human brain tissue.