A change in the internal affinity of LK goat red-cell sodium pumps induced by high pH.
The K inhibition of ouabain-sensitive ATPase activity of LK goat red cell membranes is greatly reduced at high pH. This effect is reversible, and specific, since the apparent affinities for ATP, ouabain or external K do not alter. Anti-L-treated membranes show a similar alkali-induced affinity change, but have a lower pH optimum.
D000251:Adenosine Triphosphatases / Q000097:blood; D000818:Animals; D001692:Biological Transport / Q000187:drug effects; D001693:Biological Transport, Active / Q000187:drug effects; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006041:Goats; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010042:Ouabain / Q000494:pharmacology; D011188:Potassium / Q000097:blood; D012964:Sodium / Q000097:blood*
D010042:Ouabain; D012964:Sodium; D000251:Adenosine Triphosphatases; D011188:Potassium