Abstract
The human erythrocyte membrane binds insulin through high-affinity, low-capacity binding sites (dissociation constant K d1 2.45 · 10 −9 M; capacity n 1 207 fmol/mg protein) and low-affinity, high-capacity binding sites ( K d2 0.63 · 10 −6 M; n 2 37 pmol/mg protein). Treatment of the erythrocyte membrane or the intact cells with the physiological concentration of insulin, which is within the range of K d value of the high-affinity sites, results in a significant reduction of the membrane microviscosity and the filtration time of the intact cells. Use of supraphysiological concentrations of the hormone reverses the effect of the lower concentration of insulin on the membrane microviscosity and the filtration time.
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