Abstract
A method has been devised for measuring the specific interaction of 125I-labeled human growth hormone (HGH) with microsomal membranes of rat liver. The HGH-membrane complex is isolated by centrifugation. Binding is time and temperature dependent, reversible, and saturable. In adult female rats, the maximal binding capacity of the membranes is about 0.4 pmoles HGH per mg of protein, and the dissociation constant (Kd.) of the interaction (as calculated from equilibrium data) is about 5.O × 10−10M. No significant inactivation of HGH occurs during the binding process. The pH optimum for binding is about 6.5. Membranes of young (3 days-old) rats bind 5 to 6 times less HGH than do membranes of adult (105 days-old) rats. Early data suggest that this difference with age results from a change in the number of binding sites rather than from an alteration in the affinity of the interaction.
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