Raychaudhuri P, Stringer E A, Valenzuela D M, Maitra U
J Biol Chem. 1984 Oct 10;259(19):11930-5.
A ribosomal subunit antiassociation activity has been purified from both the postribosomal supernatant and ribosomal salt-wash protein fractions of rabbit reticulocyte lysates. A majority (greater than 90%) of the activity is associated with a low molecular weight protein of Mr of approximately 25,000. A small but significant level of antiassociation activity (less than 10%) was found to be associated with higher molecular weight protein fractions. The purified 25,000-dalton antiassociation factor interacts with 60 S ribosomal subunits to prevent them from reassociating with 40 S ribosomal subunits. The factor does not seem to interact directly with 40 S subunits nor does it dissociate 80 S monosomes. The properties of this factor are thus similar to the eukaryotic initiation factor 6 isolated from both wheat germ and calf liver extracts.
已从兔网织红细胞裂解物的核糖体后上清液和核糖体盐洗蛋白组分中纯化出一种核糖体亚基抗缔合活性。大部分（超过90%）的活性与一种分子量约为25,000的低分子量蛋白质相关。发现有少量但显著水平（小于10%）的抗缔合活性与高分子量蛋白质组分相关。纯化的25,000道尔顿抗缔合因子与60 S核糖体亚基相互作用，以防止它们与40 S核糖体亚基重新缔合。该因子似乎不直接与40 S亚基相互作用，也不解离80 S单体核糖体。因此，该因子的特性类似于从小麦胚芽和小牛肝脏提取物中分离出的真核起始因子6。
