一种来自兔网织红细胞的核糖体解离因子，与起始因子M3不同。
A ribosome dissociation factor from rabbit reticulocytes distinct from initiation factor M3.
作者信息
Merrick W C, Lubsen N H, Anderson W F
出版信息
Proc Natl Acad Sci U S A. 1973 Aug;70(8):2220-3. doi: 10.1073/pnas.70.8.2220.
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-M(1), IF-M(2A), IF-M(2B), IF-M(2), 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.
一种核糖体解离因子（DF），从兔网织红细胞核糖体的0.5M KCl洗脱组分中，通过Sephadex G - 200、磷酸纤维素、DEAE - 纤维素和羟基磷灰石层析进行了纯化。最纯的制剂在3.75%丙烯酰胺凝胶上显示出一条主要带和几条次要带。在低Mg(++)浓度下的聚（U）指导的聚苯丙氨酸合成或内源性mRNA指导的珠蛋白合成中，DF不能替代IF - M(1)、IF - M(2A)、IF - M(2B)、IF - M(2)、EF - 1或EF - 2。相反，这些起始和延伸因子即使在比使多肽合成测定饱和所需水平高5 - 10倍的水平下进行测定时，也显示出很少或没有解离活性。因此，网织红细胞DF似乎是一种独特的因子。
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