Purification and characterization of mitochondrial cysteine aminotransferase from rat liver.

摘要: Cysteine aminotransferase has been purified over 300-fold from rat liver mitochondria. Transamination between L-cysteine and 2-oxoglutarate, the reverse reaction, were observed to be catalyzed by enzyme but inhibited L-aspartate. The also transamination of alanine, 3-sulfinic acid, aspartic cysteic acid. A new reaction assay method was devised, contributing an indication that mitochondrial cysteine is identical aspartate aminotransferase. latter apparently 3 reactions in degradation process within