Binding of [125I]iodobovine GH ([125I]iodo-bGH) to rat liver microsomes and Golgi/endosomal fractions isolated from male and female rats has been characterized. Binding of bGH to a pure somatogenic site was suggested by the finding that 50% inhibition of [125I]iodo-bGH binding required 5-130 ng bGH, rGH, or hGH/incubation, while around 500 ng rat PRL/incubation were needed to obtain the same effect. Binding of [125I]iodo-bGH to microsomes and Golgi/endosomes was time, temperature, and protein dependent. Maximal specific binding occurred at 15-16 and 15-20 h at 22 C in Golgi and microsomal membranes, respectively. Subcellular distribution studies demonstrated that binding sites for bGH were 20- to 25-fold concentrated in the Golgi/endosomal fractions compared to the total particulate fraction, while residual microsomes devoid of Golgi/endosomal-derived components were approximately 2-fold enriched. Low levels of somatogenic receptors were detected in lysosome-enriched fractions. Removal of endogenous ligand by treating Golgi/endosomal membranes with 3 M MgCl2 increased specific binding of bGH about 2- to 3-fold. These results indicate that approximately 50% of specific somatogenic binding sites in the low density fractions represent internalized ligand-receptor complexes. The level of rat liver somatogenic receptors did not show a pronounced sex differentiation; however, an endocrine dependence of somatogenic receptor levels is suggested by the finding that livers from rats in the late stages of pregnancy had a level of somatogenic receptors exceeding that of nonpregnant rats.
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