通过聚腺苷酸-琼脂糖亲和层析从人宫颈癌（HeLa）细胞胞质中分离出的一种蛋白质的特性分析。
Characterization of a protein species isolated from HeLa cell cytoplasm by affinity chromatography on polyadenylate-sepharose.
作者信息
Blanchard J M, Brissac C, Jeanteur P
出版信息
Proc Natl Acad Sci U S A. 1974 May;71(5):1882-6. doi: 10.1073/pnas.71.5.1882.
Abstract
Chromatography of different soluble extracts from HeLa cells on poly(A)-Sepharose columns has allowed the isolation of a protein fraction eluted by 0.2 M NaCl and localized predominantly in the cytoplasmic supernatant and in the 0.5 M KCl ribosomal wash. This fraction is present in large amounts (around 3% of total cytosolic proteins) and appears to contain a major protein species that is acidic on electrofocusing (pI around 4.5) and phosphorylated. It runs on glycerol gradients and Sephadex G-200 chromatography close to the aldolase marker (158,000 daltons) and dissociates into apparently identical subunits of 38,000 +/- 2,000 daltons on sodium dodecyl sulfate-acrylamide gels, suggesting a tetrameric structure.
摘要
对来自HeLa细胞的不同可溶性提取物在聚（A）-琼脂糖柱上进行色谱分析，已分离出一个蛋白质组分，该组分用0.2M NaCl洗脱，主要定位于细胞质上清液和0.5M KCl核糖体洗脱液中。该组分含量丰富（约占总胞质蛋白的3%），似乎含有一种主要蛋白质，在等电聚焦时呈酸性（pI约为4.5）且被磷酸化。它在甘油梯度和Sephadex G - 200色谱上的行为与醛缩酶标记物（158,000道尔顿）相近，在十二烷基硫酸钠 - 丙烯酰胺凝胶上解离为明显相同的38,000 +/- 2,000道尔顿的亚基，提示其为四聚体结构。
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