Erdmann E, Bolte H D, Schoner W
Recent Adv Stud Cardiac Struct Metab. 1975;5:351-8.
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.
细胞膜的哇巴因结合能力与(Na⁺ + K⁺)-ATP酶活性直接相关。哇巴因对(Na⁺ + K⁺)-ATP酶的抑制程度是被占据的哇巴因受体位点的一种度量。在单一物种的所有器官中,哇巴因-受体复合物的解离常数是相同的,但在不同物种之间有所不同。钾离子降低了哇巴因受体相互作用的结合速率常数,而不改变解离速率常数。用洋地黄抗体滴定豚鼠心脏中被地高辛抑制的(Na⁺ + K⁺)-ATP酶表明,在有钾离子存在的情况下,与无钾离子时相比,在较低抗体浓度下抑制作用就会逆转。得出的结论是,急性低钾血症时洋地黄不耐受反映了在这些情况下强心苷受体亲和力的增加。