Abstract

Ornithine and α-N-acetylornithine δ-aminotransferases were purified to a homogeneous state from a gramicidin S-producing strain of Bacillus brevis. Ornithine aminotransferase has a molecular weight of about 90,000 and N-acetylornithine aminotransferase has that of about 80,000 on gel filtration, respectively. Both enzymes were composed of two identical subunits. Ornithine aminotransferase is specific for ornithine, and N-acetylornithine aminotransferase is specific for N-acetylornithine as amino donor. Both enzymes used 2-oxoglutarate as amino acceptor.

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