Abstract
The binding of monomeric and polymeric [125I]hGH to rat liver plasma membranes was studied to define the characteristics of hGH binding and to explore the possible physiological significance of polymeric hGH. Monomeric and polymeric hGH, isolated from clinical grade hGH by gel filtration, represent approximately 44 and 35% of the protein in clinical gradehGH, respectively. The radioimmunoreactivity of polymeric hGH to hGH antibody was approximately 3% of that of monomeric hGH. Both polymeric and monomeric hGH bound to receptors on liver plasma membranes. Specific binding of both polymeric and monomeric hGH was similar with respect to time, affinity, temperature, pH, and monovalent cations. Binding of both polymeric and monomeric hGH was increased 4-fold by 100 DIM monovalent cation concentration. Calcium and magnesium produced a 9-fold increase in monomeric hGH binding between 10-100 mM concentration. Magnesium produced peak binding of polymeric hGH at 10 mM concentration whereas calcium produced only min...
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