Grosse F, Krauss G, Kownatzki R, Maass G
Nucleic Acids Res. 1979 Apr;6(4):1631-8. doi: 10.1093/nar/6.4.1631.
The binding between tyrosyl-tRNA synthetase (E.coli) and the alkylanalogue of the aminoacyladenylate, tyrosinyl-5'-AMP, has been investigated by fluorescence titrations and rapid mixing experiments. Tyrosyl-tRNA synthetase has two equivalent and independent binding sites for tyrosinyl-5'-AMP. The intrinsic binding constant is 4 x 10(7)M-1. The binding sites for tRNATyr and tyrosinyl-5'-AMP are independent of each other, the anticooperative mode of tRNA binding being preserved in the presence of tyrosinyl-5-AMP.
通过荧光滴定和快速混合实验研究了酪氨酰 - tRNA合成酶(大肠杆菌)与氨酰腺苷酸的烷基类似物酪氨酰 - 5'-AMP之间的结合。酪氨酰 - tRNA合成酶对酪氨酰 - 5'-AMP有两个等效且独立的结合位点。内在结合常数为4×10⁷M⁻¹。tRNATyr和酪氨酰 - 5'-AMP的结合位点相互独立,在酪氨酰 - 5-AMP存在下,tRNA结合的反协同模式得以保留。