Open AccessInteractions of a Photo-Affinity ATP Analog with Cation-Stimulated Adenosine Triphosphatases of Human Red Cell Membranes
Author(s) -
Boyd E. Haley,
Joseph F. Hoffman
Publication year - 1974
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.71.9.3367
Subject(s) - membrane , adenosine triphosphate , atp hydrolysis , atpase , ouabain , adenosine , biochemistry , chemistry , ultraviolet light , f atpase , cell membrane , red cell , biophysics , covalent bond , enzyme , biology , sodium , photochemistry , thylakoid , organic chemistry , chloroplast , computer security , computer science , gene
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.
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