Bloch S, Ledig M, Mandel P, Tholey G
C R Acad Sci III. 1984;298(6):127-30.
A procedure for the isolation and purification to homogeneity of glutamine synthetase (E.C. 6.3.1.2.) from chick brain is described. The physico-chemical properties of the purified enzyme preparation are similar to those of other eucaryotic glutamine synthetases. The optimum activity of glutamine synthetase is dependent on the Mg++ to ATP ratio in the reaction mixture rather than on the magnesium or ATP concentrations. The characteristics of the enzyme studied through various phylogenetic trees suggest that this enzyme is preserved during evolution.
本文描述了一种从鸡脑中分离纯化谷氨酰胺合成酶（E.C. 6.3.1.2.）并使其达到同质的方法。纯化酶制剂的物理化学性质与其他真核生物谷氨酰胺合成酶相似。谷氨酰胺合成酶的最佳活性取决于反应混合物中Mg++与ATP的比例，而不是镁或ATP的浓度。通过各种系统发育树研究该酶的特性表明，这种酶在进化过程中得以保留。
