Purification and properties of glutamine phosphoribosylpyrophosphate amidotransferase from Bacillus subtilis.
Purification and properties of glutamine phosphoribosylpyrophosphate amidotransferase from Bacillus subtilis.
复制标题
枯草芽孢杆菌谷氨酰胺磷酸核糖焦磷酸酰胺转移酶的纯化和性质。
DOI：
10.1021/bi00523a005
复制
发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Switzer,RL
中科院分区：
文献类型：
--
作者：
Wong,JY;Bernlohr,DA;Turnbough,CL;Switzer,RL
Joseph Y. Wong、David A. Bernlohr、Charles L. Turnbough* 和 Robert L. Switzer* 摘要：描述了一种从去抑制的枯草芽孢杆菌细胞中快速有效纯化谷氨酰胺磷酸核糖焦磷酸酰胺转移酶的方法，其同质性高于 98%。该亚基的分子量估计约为 50 000。纯化的酶在高分辨率聚丙烯酰胺凝胶电泳上表现出微异质性；有人认为这种异质性是由于天然亚基的有限蛋白水解修饰造成的。天然酶以四聚体、二聚体和单体形式平衡存在。 (jlutamine磷酸核糖焦磷酸酰胺转移酶的影响
Joseph Y. Wong, David A. Bernlohr, Charles L. Turnbough,* and Robert L. Switzer* abstract: A procedure for the rapid and efficientpurification of glutamine phosphoribosylpyrophosphate amidotransferase to better than 98% homogeneity from derepressed Bacillus subtilis cells is described. The molecular weight of the subunit was estimated to be about 50 000. The purified enzyme ex-hibits microheterogeneity on electrophoresis on highly resolving polyacrylamide gels; it is suggested that this heterogeneity results from limited proteolytic modification of the native subunit. The native enzyme exists in equilibrium among tetrameric, dimeric, and monomeric forms. The influence of (jlutamine phosphoribosylpyrophosphate amidotransferase