Sonenberg N, Rupprecht K M, Hecht S M, Shatkin A J
Proc Natl Acad Sci U S A. 1979 Sep;76(9):4345-9. doi: 10.1073/pnas.76.9.4345.
A 24,000-dalton polypeptide that binds strongly and can be specifically crosslinked to the 5'-terminal cap structure m7GpppN in eukaryotic mRNAs has been detected in protein synthesis initiation factor preparations [Proc. Natl. Acad. Sci. USA (1978) 75, 4843--4847]. This polypeptide has been purified to apparent homogeneity by one chromatographic passage through an affinity resin prepared by coupling the levulinic acid O2',3'-acetal of m7GDP to AH-Sepharose 4B. Translation, in HeLa cell extracts, of capped mRNAs including Sindbis virus, reovirus, and rabbit globin mRNAs was stimulated by the cap-binding protein under conditions that did not increase translation of noncapped RNAs of encephalomyocarditis virus and satellite tobacco necrosis virus.
在蛋白质合成起始因子制剂中已检测到一种24000道尔顿的多肽，它能与真核生物mRNA中的5'-末端帽结构m7GpppN紧密结合并能被特异性交联[美国国家科学院院刊(1978年)75, 4843 - 4847]。通过一次色谱层析，使该多肽通过将m7GDP的乙酰丙酸O2',3'-缩醛偶联到AH - Sepharose 4B制备的亲和树脂，已将其纯化至表观均一性。在不增加脑心肌炎病毒和烟草坏死卫星病毒非加帽RNA翻译的条件下，帽结合蛋白可刺激在HeLa细胞提取物中对包括辛德毕斯病毒、呼肠孤病毒和兔珠蛋白mRNA在内的加帽mRNA进行翻译。
