Kaufmann E
MRC Laboratory of Molecular Biology, Cambridge, England.
Protein Expr Purif. 1990 Nov;1(2):191-5. doi: 10.1016/1046-5928(90)90015-q.
A crude cell extract from yeast Saccharomyces cerevisae was fractionated by affinity chromatography using the leucine tRNA gene as the recognition site. This approach enables the rapid purification of a protein, which retained its full DNA binding capacity during the enrichment procedure. The active fraction contains two major polypeptides of 140 and 170 kDa and a minor component of 100 kDa. The 170-kDa component does not bind to the DNA. The likelihood that the DNA binding protein is one of the components of transcription factor tau is discussed.
利用亮氨酸tRNA基因作为识别位点，通过亲和层析对酿酒酵母的粗细胞提取物进行了分级分离。这种方法能够快速纯化一种蛋白质，该蛋白质在富集过程中保留了其完整的DNA结合能力。活性组分包含两条主要的多肽，分子量分别为140 kDa和170 kDa，以及一个分子量为100 kDa的次要组分。170 kDa的组分不与DNA结合。文中讨论了DNA结合蛋白是转录因子tau的组分之一的可能性。
