Steiner R F
Arch Biochem Biophys. 1984 Jan;228(1):105-12. doi: 10.1016/0003-9861(84)90051-1.
The quenching by radiationless energy transfer of the ultraviolet fluorescence of Tyr-99 and Tyr-138 by bound 1-anilinonaphthalene-8-sulfonate (1,8-ANS) has been employed to determine the separation of a hydrophobic binding site of 1,8-ANS from each of the tyrosines. The results suggest that the dominant binding site is located in the N-terminal region of domain III.
通过结合的1-苯胺基萘-8-磺酸盐(1,8-ANS)对Tyr-99和Tyr-138的紫外荧光进行无辐射能量转移猝灭,已用于确定1,8-ANS的疏水结合位点与每个酪氨酸之间的距离。结果表明,主要结合位点位于结构域III的N端区域。