Konziase Benetode
Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamada-oka, Suita, Osaka 565-0871, Japan.
Data Brief. 2015 Oct 3;5:383-7. doi: 10.1016/j.dib.2015.09.026. eCollection 2015 Dec.
Here we describe the isolation and purity determination of Trypanosoma brucei (T. b.) brucei candidate target proteins of artemisinin. The candidate target proteins were detected and purified from their biological source (T. b. brucei lysate) using the diazirine-free biotinylated probe 5 for an affinity binding to a streptavidin-tagged resin and, subsequently, the labeled target proteins were purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). We herein showed the electrophoresis gel and the immunoblotting film containing the 60-kDa trypanosomal candidate target protein of artemisinin as a single band, which was visualized on-gel by the reverse-staining method and on a Western blotting film by enhanced chemiluminescence. The data provided in this article are related to the original research article "Biotinylated probes of artemisinin with labeling affinity toward Trypanosoma brucei brucei target proteins", by Konziase (Anal. Biochem., vol. 482, 2015, pp. 25-31. http://dx.doi.org/10.1016/j.ab.2015.04.020).
在此，我们描述了布氏锥虫中青蒿素候选靶蛋白的分离及纯度测定。使用无重氮丙啶生物素化探针5从其生物来源（布氏锥虫裂解物）中检测并纯化候选靶蛋白，使其与链霉亲和素标记的树脂进行亲和结合，随后，通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）纯化标记的靶蛋白。我们在此展示了含有60 kDa青蒿素锥虫候选靶蛋白的电泳凝胶和免疫印迹膜，其呈现为单一条带，通过反向染色法在凝胶上可视化，并通过增强化学发光法在Western印迹膜上可视化。本文提供的数据与Konziase的原始研究文章《对布氏锥虫靶蛋白具有标记亲和力的青蒿素生物素化探针》（《分析生物化学》，第482卷，2015年，第25 - 31页。http://dx.doi.org/10.1016/j.ab.2015.04.020）相关。
