Glutamic-glycine Transaminase from Rat Liver.

.ilthough there is ample evidence for the existence of many different transaminases, the lack of progress in the separation of more individually specific transaminases has been lamented by reviewers for a number of years. Transaminations involving glycine or glyoxylate have been studied extensively in crude preparations of animal (1, 2), plants (3), and microorganisms (4), as well as with purified enzymes (5-8) and in nonenzymatic systems (9, 10). The only purified transaminases reported to be capable of converting glyoxylate to glycine are the ornithine, glutamine, and asparagine enzymes described by Meister et al. (5-8). The glutamine transaminase is functionally irreversible because of concurrent deamidation, but the asparagine enzyme has been shown to be reversible and includes glycine among the amino group donors. In this communication, we wish to report briefly on the partial purificat’ion and properties of a glutamic-glycine transaminase.