用人胎盘纯化的精氨酰 - tRNA合成酶识别各种精氨酸转移核糖核酸。
Recognition of various arginine transfer ribonucleic acids with arginyl-tRNA synthetase purified from human placenta.
作者信息
Katon N, Saneyoshi M
出版信息
Nucleic Acids Symp Ser. 1979(6):s119-22.
Arginyl-tRNA synthetase has been purified approximately 550 fold from crude extract of human placenta by the following purification steps: Ammonium sulfate fractionation, chromatographies of DEAE-cellulose and CM-Sephadex and Sephadex G-100 gel filtration. Final preparation of this enzyme has specific activity of 123 nmole of arginyl-tRNA formed per mg of protein and was free from other aminoacyl-tRNA synthetase activities. Recognition of various arginine tRNAs with this enzyme was studied using kinetic analysis of arginylation of arginine tRNA and also arginine tRNA dependent ATP-PPi exchange reaction. Affinity of this enzyme with arginine tRNA was determine from Vmas/Km values and it was in the order of rabbit, Chum salmon, B. subtilis, E. coli and yeast in both systems.
通过以下纯化步骤，已从人胎盘粗提物中将近似550倍纯化精氨酰 - tRNA合成酶：硫酸铵分级分离、DEAE - 纤维素和CM - 葡聚糖凝胶色谱以及葡聚糖G - 100凝胶过滤。该酶的最终制剂具有每毫克蛋白质形成123纳摩尔精氨酰 - tRNA的比活性，且不含其他氨酰 - tRNA合成酶活性。使用精氨酸tRNA的精氨酰化动力学分析以及精氨酸tRNA依赖性ATP - PPi交换反应，研究了该酶对各种精氨酸tRNA的识别。通过Vmas/Km值确定该酶与精氨酸tRNA的亲和力，在两个系统中其顺序均为兔、大麻哈鱼、枯草芽孢杆菌、大肠杆菌和酵母。
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