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Ouabain binding capacity of cell membranes is directly related to (Na+ + K+)-ATPase activity. The extent of ouabain inhibition of (Na+ + K+)-ATPase is a measure of ouabain receptor sites occupied. Dissociation constants of the ouabain-receptor complexes are identical in all organs in a single species but vary among different species. K+ decreases the association rate constant of the ouabain receptor interaction without altering the dissociation rate constants. Titration of digoxin-inhibited (Na+ + K+)-ATPase from guinea pig heart with digoxin antibodies shows a reversal of the inhibition at lower antibody concentrations in the presence of K+ than in the absence of K+. It is concluded that digitalis intolerance in acute hypokalemia reflects the increased affinity of the cardiac glycoside receptor under these conditions.
E Erdmann, and
H D Bolte, and
W Schoner
March 1959,
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E Erdmann, and
H D Bolte, and
W Schoner
March 1974,
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E Erdmann, and
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W Schoner
January 1972,
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E Erdmann, and
H D Bolte, and
W Schoner
June 1972,
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E Erdmann, and
H D Bolte, and
W Schoner
January 1975,
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E Erdmann, and
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W Schoner
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E Erdmann, and
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W Schoner
June 1995,
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E Erdmann, and
H D Bolte, and
W Schoner
November 1956,
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E Erdmann, and
H D Bolte, and
W Schoner
January 1983,
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E Erdmann, and
H D Bolte, and
W Schoner
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Clinical cardiology,
