大鼠肝脏L-苏氨酸脱氨酶的一级结构。
Primary structure of rat liver L-threonine deaminase.
作者信息
Leoncini R, Henschen A, Krieglstein K, Calvete J, Pagani R, Marinello E
机构信息
Istituto di Chimica Biologica, Università, Siena.
出版信息
Ital J Biochem. 1990 Jul-Aug;39(4):228-34.
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.
利用从雄性Wistar大鼠获得的高度纯化制剂（比活性=940 U/mg蛋白质）研究了大鼠肝脏L-苏氨酸脱氨酶的一级结构。这些数据已与其他作者获得的预测序列进行了比较，结果表明与野田的预测相当一致，与小川的结果存在差异。快原子轰击质谱分析表明，在N端丙氨酸上存在一个作为封闭剂的乙酰基。
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