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Rat reticulocytes possess receptors for an insulin-like somatomedin peptide ILAs. At 20 C, pH 7.4 and 10(8) cells per ml, the binding of 125I-ILAs reached a steady-state at 120 min. Binding was partially reversible at 20 C and totally reversible at 37 C. Insulin did not compete with ILAs at concentrations as high as 10 microgram/ml. Insulin-like growth factor II (IGF II) competed with the same potency as ILAs itself, while insulin-like growth factor I (IGF I) was five times less potent. The optimum pH for 125I-ILAs binding was 8.5. Mature erythrocytes possessed seven times less binding sites than reticulocytes. These data suggest that the somatomedins might mediate the effect of growth hormone on erythropoiesis.
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