Threadgill G J, Conrad R C, Cannon M, Craven G R
Laboratory of Molecular Biology, University of Wisconsin-Madison 53706.
Biochem J. 1987 Jun 15;244(3):523-32. doi: 10.1042/bj2440523.
Ribosomal proteins from the yeast Saccharomyces cerevisiae were separated, on a preparative scale, by ion-exchange h.p.l.c. Proteins from the small and large ribosomal subunits were resolved, respectively, into 33 and 23 peaks, and most of the proteins present in these peaks were identified by using one- and two-dimensional gel electrophoresis. Several of the peaks appeared to contain a single protein uncontaminated by other species. Ribosomal proteins were also separated by using reverse-phase h.p.l.c. Analysis of the peaks resolved indicated that the order of elution for the proteins of both ribosomal subunits is, in certain cases, different for each of the two h.p.l.c. techniques used. Thus a combination of the two chromatographic methods employed here has the potential to facilitate the rapid and preparative separation of each of the proteins present in yeast ribosomes.
通过离子交换高效液相色谱法，对酿酒酵母的核糖体蛋白进行了制备规模的分离。来自小核糖体亚基和大核糖体亚基的蛋白分别被分离成33个和23个峰，并且通过一维及二维凝胶电泳鉴定了这些峰中存在的大多数蛋白。其中几个峰似乎只含有单一蛋白，未被其他种类污染。核糖体蛋白也通过反相高效液相色谱法进行了分离。对分离出的峰的分析表明，在某些情况下，对于所使用的两种高效液相色谱技术中的每一种，两个核糖体亚基的蛋白洗脱顺序都不同。因此，这里采用的两种色谱方法相结合，有可能促进酵母核糖体中存在的每种蛋白的快速制备分离。
