Billheimer J T, Carnevale H N, Leisinger T, Eckhardt T, Jones E E
J Bacteriol. 1976 Sep;127(3):1315-23. doi: 10.1128/jb.127.3.1315-1323.1976.
Procedures that have been developed for the purification of acetylornithine delta-transaminase from Escherichia coli W also lead to the simultaneous purification of ornithine delta-transaminase. These two enzymatic activities have the same electrophoretic mobility and are identical immunochemically. Studies of inhibition kinetics demonstrate that the two substrates, acetylornithine and ornithine, compete for the same active site of acetylornithine delta-transaminase; thus, the ornithine delta-transaminase activity in E coli is due to acetylornithine delta-transaminase and not to a separate specific ornithine delta-transaminase.
已开发出的从大肠杆菌W中纯化乙酰鸟氨酸δ-转氨酶的方法,同时也能纯化鸟氨酸δ-转氨酶。这两种酶活性具有相同的电泳迁移率,并且在免疫化学上是相同的。抑制动力学研究表明,两种底物乙酰鸟氨酸和鸟氨酸竞争乙酰鸟氨酸δ-转氨酶的同一活性位点;因此,大肠杆菌中的鸟氨酸δ-转氨酶活性是由于乙酰鸟氨酸δ-转氨酶,而不是由于一种单独的特异性鸟氨酸δ-转氨酶。