Moelling K, Sykora K W, Dittmar K E, Scott A, Watson K F
J Biol Chem. 1979 May 25;254(10):3738-42.
From the same batch of virus, the four major avian viral structural proteins p27, p19, p15, and p12, the reverse transcriptase, the envelope glycoprotein gp85, and the high molecular weight 70 S RNA have been recovered. All proteins, except for gp85, have been purified by use of column chromatography procedures to apparent homogeneity as judged by sodium dodecyl sulfate-polyacrylamide gels and isoelectric focusing. A new isolation procedure for p12 by affinity column chromatography takes advantage of its nucleic acid binding properties. The recovery of nondenatured viral structural proteins is demonstrated by the proteolytic activity revealed by p15. The purified proteins were used for the production of monospecific antibodies. The 70 S RNA served as source for the isolation of 35 S RNA subunits.
从同一批病毒中，已分离出四种主要的禽病毒结构蛋白p27、p19、p15和p12、逆转录酶、包膜糖蛋白gp85以及高分子量70S RNA。除gp85外，所有蛋白质均通过柱色谱法纯化至表观均一，这是通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和等电聚焦判断的。通过亲和柱色谱法分离p12的新方法利用了其核酸结合特性。p15所显示的蛋白水解活性证明了未变性病毒结构蛋白的回收。纯化后的蛋白质用于制备单特异性抗体。70S RNA用作分离35S RNA亚基的来源。
