6-去甲基金霉素与70S、50S和30S核糖体颗粒的结合：荧光偏振定量研究。
The binding of 6-demethylchlortetracycline to 70S, 50S and 30S ribosomal particles: a quantitative study by fluorescence anisotropy.
作者信息
Epe B, Woolley P
出版信息
EMBO J. 1984 Jan;3(1):121-6. doi: 10.1002/j.1460-2075.1984.tb01771.x.
Abstract
The binding of demeclocycline (6-demethylchlortetracycline) to ribosomes and ribosomal subunits from Escherichia coli was investigated by using the fluorescence anisotropy of the antibiotic to determine the extent of binding. Binding data obtained from 70S and 30S particles differed fundamentally from those obtained from 50S subunits: the first two showed a strong, specific interaction while the third did not. In addition, all three particles possessed weak, unspecific binding sites. Computer-aided least-squares analysis of the data yielded the following numbers of sites and equilibrium constants: for 30S, n1 = 1, K1 = 2.2 X 10(6) M-1, n2 K2 = 0.029 X 10(6) M-1; for 50S, n1 = 0, n2 K2 = 0.035 X 10(6) M-1; for 70S, n1 = 1, K1 = 3.2 X 10(6) M-1, n2 K2 = 0.082 X 10(6) M-1. These data resolve current disagreement in the literature and are a prerequisite for quantitative studies of the mechanism of inhibition by tetracycline of protein biosynthesis.
摘要
通过利用地美环素（6-去甲基金霉素）的荧光各向异性来测定其结合程度，研究了地美环素与大肠杆菌核糖体及核糖体亚基的结合情况。从70S和30S颗粒获得的结合数据与从50S亚基获得的数据有根本差异：前两者表现出强烈的特异性相互作用，而后者则没有。此外，所有三种颗粒都具有弱的非特异性结合位点。对数据进行计算机辅助最小二乘法分析得出以下位点数量和平衡常数：对于30S，n1 = 1，K1 = 2.2×10⁶ M⁻¹，n2K2 = 0.029×10⁶ M⁻¹；对于50S，n1 = 0，n2K2 = 0.035×10⁶ M⁻¹；对于70S，n1 = 1，K1 = 3.2×10⁶ M⁻¹，n2K2 = 0.082×10⁶ M⁻¹。这些数据解决了文献中目前存在的分歧，并且是对四环素抑制蛋白质生物合成机制进行定量研究的前提条件。
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