大肠杆菌核糖体蛋白S4、S7、S8、S15、S17和S20与16S RNA结合的表观缔合常数。
Apparent association constants for E. coli ribosomal proteins S4, S7, S8, S15, S17 and S20 binding to 16S RNA.
作者信息
Schwarzbauer J, Craven G R
出版信息
Nucleic Acids Res. 1981 May 11;9(9):2223-37. doi: 10.1093/nar/9.9.2223.
Abstract
We have previously reported the development of a technique utilizing nitrocellulose filters, which rapidly separates ribosomal protein-ribosomal RNA complexes from unbound protein. We have used this technique to obtain binding data for the association of proteins S4, S7, S8, S15, S17, and S20 with 16S RNA. With the exception of protein S17, the association behavior for each of these proteins exhibits a single binding site with a unique binding constant. The apparent association constants have been calculated and have been found to have a range from 1.6 x 10(6) M-1 for protein S7 to 7.1 x 10(7) M-1 for protein S17. The Scatchard plot for the protein S17 binding data is biphasic, suggesting that within the RNA population two different binding sites exist, each with a different apparent association constant.
摘要
我们之前报道了一种利用硝酸纤维素滤膜的技术的开发，该技术能迅速将核糖体蛋白 - 核糖体RNA复合物与未结合的蛋白分离。我们已使用此技术获得了蛋白质S4、S7、S8、S15、S17和S20与16S RNA结合的数据。除了蛋白质S17外，这些蛋白质中的每一种的结合行为都表现出具有独特结合常数的单一结合位点。已计算出表观结合常数，发现其范围从蛋白质S7的1.6×10⁶ M⁻¹到蛋白质S17的7.1×10⁷ M⁻¹。蛋白质S17结合数据的Scatchard图是双相的,这表明在RNA群体中存在两个不同的结合位点，每个位点具有不同的表观结合常数。
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