Abstract
Abstract—Aromatic: 2‐oxoglutarate aminotransferase has been purified about 950‐fold from rat brain mitochondria. The purified enzyme was homogeneous in polyacrylamide gel electrophoresis and had a molecular weight of approx 63,000. On the basis of substrate specificity, substrate inhibition, purification ratio, yield, polyacrylamide gel electrophoresis and some other properties of the enzyme it has been suggested that brain mitochondrial tyrosine:2‐oxoglutarate aminotransferase (l‐tyrosine: 2‐oxoglutarate aminotransferase, EC 2.6.1.5) is identical with brain mitochondrial phenylalanine and kynurenine: 2‐oxoglutarate aminotransferases (l‐kynurenine: 2‐oxoglutarate aminotransferase, EC 2.6.1.7), and also with aspartate: 2‐oxoglutarate aminotransferase (l‐aspartate: 2‐oxoglutarate aminotransferase, EC 2.6.1.1).
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