Does the conformation of Mg-ATPase (spectrin-dependent ATPase) influence the passive permeability to K+?
The processing of human erythrocytes disclosed changes in Mg-ATPase activity following action of Pb2+ and Nile blue, and changes of permeability of K+ after treatment with Nile blue. The obtained results and those from previous papers can be summarized as follows : Substances decreasing the activity of stimulated membrane Mg-ATPase (spectrin-dependent ATPase) in red blood cells increase the passive permeability to K+, and substances increasing the stimulated Mg-ATPase activity decrease the passive permeability to K+. A hypothesis is proposed that the conformation of Mg-ATPase is secondarily reflected in the state of the proper path for K+ transport through the membrane; thus the rate of passive permeability to K+ is influenced.
D000251:Adenosine Triphosphatases / Q000097:blood*; D001693:Biological Transport, Active / Q000187:drug effects; D017301:Ca(2+) Mg(2+)-ATPase; D002463:Cell Membrane Permeability / Q000187:drug effects; D004912:Erythrocytes / Q000187:drug effects / Q000201:enzymology*; D006801:Humans; D007854:Lead / Q000494:pharmacology; D008565:Membrane Proteins / Q000378:metabolism*; D010042:Ouabain / Q000494:pharmacology; D010078:Oxazines / Q000494:pharmacology; D011188:Potassium / Q000097:blood*; D011487:Protein Conformation; D012503:Saponins / Q000494:pharmacology; D012964:Sodium / Q000097:blood; D013049:Spectrin / Q000378:metabolism*
D008565:Membrane Proteins; D010078:Oxazines; D012503:Saponins; D013049:Spectrin; C008619:Nile Blue; D007854:Lead; D010042:Ouabain; D012964:Sodium; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; D011188:Potassium