Lefevre J F, Ehrlich R, Remy P
Eur J Biochem. 1980 Jan;103(1):155-9. doi: 10.1111/j.1432-1033.1980.tb04299.x.
The variations of several spectroscopic properties of yeast tRNA-Phe and phenylalanyl-tRNA synthetase upon complex formation, were used to study the stoichiometry of the complex in different experimental conditions. In all cases, for the tRNA-Phe-enzyme complex, in the absence of other ligands, the saturations of the different conformational changes monitored for both macromolecules, are achieved at a 2:1 tRNA/enzyme stoichiometry. Phenylalanine does not modify this saturation. In contrast, the presence of 1 mM ATP induces an asymmetric behaviour of the synthetase: two tRNAs are still bound per enzyme molecule but the conformational change of the latter is completed upon binding of a single tRNA molecule.
利用酵母苯丙氨酸转运核糖核酸（tRNA-Phe）和苯丙氨酰-tRNA合成酶在形成复合物时几种光谱性质的变化，来研究在不同实验条件下复合物的化学计量比。在所有情况下，对于tRNA-Phe-酶复合物，在没有其他配体的情况下，两种大分子监测到的不同构象变化的饱和度，在tRNA/酶化学计量比为2:1时达到。苯丙氨酸不会改变这种饱和度。相反，1 mM三磷酸腺苷（ATP）的存在会诱导合成酶的不对称行为：每个酶分子仍结合两个tRNA，但后者的构象变化在结合单个tRNA分子时就完成了。
