Interactions of a Photo-Affinity ATP Analog with Cation-Stimulated Adenosine Triphosphatases of Human Red Cell Membranes
AUTOR(ES)
Haley, Boyd E.
RESUMO
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 (N3ATP). In the absence of ultraviolet light it is a substrate for both the Mg-ATPase and the ouabain-sensitive, Na,K-ATPase. Hydrolysis of N3ATP is prevented by increasing concentrations of ATP. Photolysis of N3ATP 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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=433773Documentos Relacionados
- Cation-stimulated Adenosine Triphosphatase Activity and Cation Transport in Corn Roots
- Photo-Affinity Labels for Adenosine 3′:5′-Cyclic Monophosphate
- Photo-affinity labels for adenosine 3′:5′-cyclic monophosphate
- Photo-Affinity Labeling of Specific Acetylcholine-Binding Sites on Membranes
- Identification by Photo-Affinity Labeling of the Proteins in Escherichia coli Ribosomes Involved in Elongation Factor G-Dependent GDP Binding