Mirsalikhova N M, Gussakovskiĭ E E, Burkhanov S, Ziiamukhamedov R A, Tashmukhamedov B A
Biofizika. 1975 Nov-Dec;20(6):980-6.
On the strength of the study of tryptophan fluorescence of Na+, K+-ATPase preparation a conclusion about conformational changes of the enzume molecule at the level of its tertiary structure is made. The largest changes of intensity and position of fluorescence spectrum consequently the macromolecule structure are discovered at the formation of Mg-ATP-enzyme complex.
基于对Na +，K + -ATP酶制剂色氨酸荧光的研究，得出了关于该酶分子三级结构水平构象变化的结论。在Mg-ATP-酶复合物形成时，发现荧光光谱强度和位置的最大变化，进而发现大分子结构的最大变化。
