Measurement of specific [3H]-ouabain binding to different types of human leucocytes.

Journal article

We have studied the specific binding of [3H]-ouabain to intact mononuclear leucocytes (82% lymphocytes) and polymorphonuclear leucocytes. In both types of cells [3H]-ouabain binding was saturable, confined to a single site of high affinity, slow to reach equilibrium, slow to reverse, temperature-dependent, competitively antagonized by potassium, and facilitated by the presence of divalent cations. The equilibrium dissociation constants were 2.4 +/- 0.7 nmol/l (polymorphs) and 2.4 +/- 0.4 nmol...

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Authors: Boon, N; Oh, V; Taylor, E; Johansen, T; Aronson, J

• Publication status: Published
• Journal: British journal of clinical pharmacology
• Volume: 18
• Issue: 2
• Pages: 153-161
• Publication date: 1984-08-01
• DOI: 10.1111/j.1365-2125.1984.tb02447.x
• EISSN: 1365-2125
• ISSN: 0306-5251
• Language: English
• Keywords: Sodium-Potassium-Exchanging ATPase; Kinetics; Cations, Divalent; Monocytes; Neutrophils; Potassium; Temperature; Receptors, Drug; Digoxin; Humans; Ouabain; Leukocytes; Centrifugation, Density Gradient; Binding, Competitive