期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1973
卷号：70
期号：8
页码：2220-2223
DOI：10.1073/pnas.70.8.2220
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：A ribosome dissociation factor (DF), from a 0.5 M KCl wash fraction of rabbit-reticulocyte-ribosomes, has been purified by Sephadex G-200, phosphocellulose, DEAE-cellulose, and hydroxyapatite chromatography. The most purified preparation displayed one major and several minor bands on 3.75% acrylamide gels. DF cannot replace IF-M1, IF-M2A, IF-M2B, IF-M2, EF-1, or EF-2 in poly(U)-directed polyphenylalanine synthesis at low Mg++ concentrations or in endogenous mRNA-directed globin synthesis. Conversely, these initiation and elongation factors showed little or no dissociation activity, even when assayed at levels 5-10 times greater than those required to saturate a polypeptide synthesis assay. Reticulocyte DF thus appears to be a distinct factor.
关键词：elongation factors ; protein synthesis ; sucrose density gradients ; protein purification
