Purification and subunit structure of deoxyribonucleic acid-dependent ribonucleic acid polymerase III from the mouse plasmacytoma, MOPC 315.
Purification and subunit structure of deoxyribonucleic acid-dependent ribonucleic acid polymerase III from the mouse plasmacytoma, MOPC 315.
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来自小鼠浆细胞瘤 MOPC 315 的脱氧核糖核酸依赖性核糖核酸聚合酶 III 的纯化和亚基结构。
DOI：
10.1016/s0021-9258(17)33802-4
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发表时间：
1975
期刊：
影响因子：
--
通讯作者：
R. Roeder
中科院分区：
文献类型：
--
作者：
V. E. Sklar;R. Roeder
Class III DNA-dependent RNA polymerases were purified from the mouse plasmacytoma, MOPC 315. RNA polymerases IIIA and IIIB were solubilized from a whole cell extract and resolved by chromatography on DEAE-Sephadex. Chromatography on DEAE-cellulose, DEAE-Sephadex, CM-Sephadex, and phosphocellulose ion exchange resins and sedimentation in sucrose density gradients yielded chromatographically homogeneous Enzymes IIIA and IIIB which were purified approximately 22,000 and 53,000-fold respectively, relative to whole cell extracts. The specific activity of these enzymes was comparable to that reported for other purified eukaryotic RNA polymerases. Sucrose gradient sedimentation analysis suggested a molecular weight of approximately 650,000 for each of the class III enzymes.
