Simultaneous purification and some properties of aspartate: tRNA ligase and seven other amino-acid:tRNA ligases from Escherichia coli.
Simultaneous purification and some properties of aspartate: tRNA ligase and seven other amino-acid:tRNA ligases from Escherichia coli.
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来自大肠杆菌的天冬氨酸：tRNA 连接酶和其他七种氨基酸：tRNA 连接酶的同时纯化和一些特性。
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发表时间：
1978
期刊：
影响因子：
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通讯作者：
L. Lundvik
中科院分区：
文献类型：
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作者：
B. Akesson;L. Lundvik
本文描述了一种从大肠杆菌中纯化天冬氨酸：tRNA连接酶的方法，该方法通过聚丙烯酰胺凝胶电泳将其纯化到均一的阶段。从同一批E.大肠杆菌中，赖氨酸、苯丙氨酸和丝氨酸连接酶以明显均质的形式获得，而丙氨酸、谷氨酰胺、亮氨酸和缬氨酸酶的纯度在20%至80%之间变化。天冬氨酸：tRNA连接酶，这还没有得到一个高度纯化的形式之前，其特征在于在其分子参数。
A procedure is described for the purification of the aspartate:tRNA ligase from Escherichia coli to a stage where it was homogeneous by polyacrylamide gel electrophoresis. From the same batch of E. coli the lysine, phenylalanine and serine ligases were obtained in an apparently homogeneous form while the alanine, glutamine, leucine and valine enzymes had a purity varying from 20% to 80%. Aspartate: tRNA ligase, which has not been obtained in a highly purified form before, has been characterized in terms of its molecular parameters.