Haley B E, Hoffman J F
Proc Natl Acad Sci U S A. 1974 Sep;71(9):3367-71. doi: 10.1073/pnas.71.9.3367.
To identify and isolate ATP binding and hydrolyzing sites of human red cell membranes we have synthesized a photo-activated ATP analog, 8-azido adenosine triphosphate (N(3)ATP). In the absence of ultraviolet light it is a substrate for both the Mg-ATPase and the ouabain-sensitive, Na,K-ATPase. Hydrolysis of N(3)ATP is prevented by increasing concentrations of ATP. Photolysis of N(3)ATP with red cell membranes results in covalent incorporation and irreversible inhibition of both ATPase activities. Also, only three protein components of the red cell membranes are labeled. This labeling is completely abolished by appropriate concentrations of ATP.
为了鉴定和分离人红细胞膜的ATP结合与水解位点,我们合成了一种光活化的ATP类似物,即8-叠氮腺苷三磷酸(N(3)ATP)。在没有紫外线的情况下,它是镁-ATP酶和哇巴因敏感的钠钾-ATP酶的底物。ATP浓度增加可阻止N(3)ATP的水解。N(3)ATP与红细胞膜进行光解反应会导致共价结合并对两种ATP酶活性产生不可逆抑制。此外,红细胞膜中只有三种蛋白质成分被标记。适当浓度的ATP可完全消除这种标记。