SOLUBILIZATION OF A GROWTH HORMONE-SPECIFIC RECEPTOR FROM RABBIT LIVER

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Abstract
Membrane preparations from rabbit liver, known to possess GH [growth hormone]-specific binding sites, were solubilized with Triton X-100 and the binding characteristics of [125I]-human GH (hGH) and [125I]-bovine GH (bGH) were subsequently studied. Specific binding of the hGH and bGH by the solubilized preparation was demonstrated by separation of bound and free hormone by either polyethylene glycol precipitation or by Sephadex G-100 chromatography. Binding of hGH was both rapid and reversible and was displaced only by other growth hormones (bovine and ovine) and not by lactogenic hormones (ovine and human prolactins, human placental lactogen). As shown by Scatchard analysis specific binding of [125I]-bGH exhibited a lower binding affinity and capacity than did [125I]-hGH. Overall, the characteristics of the binding reaction for hGH were not significantly different from those reported for the particulate membrane preparation. The solubilization process did not appear to alter the binding protein(s) therefore, and permits a further study of the isolation, purification and properties of the binding protein(s) itself.