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The primary structure of rat liver L-threonine deaminase has been studied utilizing a highly purified preparation (S.A. = 940 U/mg protein) obtained from Wistar male rats. These data have been compared with the predicted sequences obtained by other Authors, showing a considerable concordance with the Noda's prediction and difference with the Ogawa's results. The FAB-MS analysis has demonstrated the presence of an acetyl group as blocking agent on the N-terminal alanine.
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