Interactions of a photo-affinity ATP analog with cation-stimulated adenosine triphosphatases of human red cell membranes.
Interactions of a photo-affinity ATP analog with cation-stimulated adenosine triphosphatases of human red cell membranes.
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光亲和 ATP 类似物与人红细胞膜的阳离子刺激的腺苷三磷酸酶的相互作用。
DOI：
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发表时间：
1974
影响因子：
11.1
通讯作者：
J. Hoffman
中科院分区：
文献类型：
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作者：
B. Haley;J. Hoffman
为了识别和分离人红细胞膜的 ATP 结合和水解位点，我们合成了光激活 ATP 类似物，8-叠氮三磷酸腺苷 (N(3)ATP)。在没有紫外线的情况下，它是 Mg-ATP 酶和哇巴因敏感的 Na,K-ATP 酶的底物。增加 ATP 浓度可防止 N(3)ATP 水解。 N(3)ATP 与红细胞膜的光解导致两种 ATP 酶活性的共价结合和不可逆抑制。此外，仅标记了红细胞膜的三种蛋白质成分。适当浓度的 ATP 可以完全消除这种标记。
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.