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- W2138777783 abstract "The specific binding of a GRF radioligand, [His1,125I-Tyr10,Nle27]hGRF-l-32NH2, to rat pituitary homogenates is reduced by the addition of GTP and its nonhydrolyzable analogs 5'-guanylylimidodiphosphate (GppNHp) and guanosine 5'-O-(3-thiotriphosphate) (GTP-γ-S). GDP and cAMP had no effect while the nonhydrolyzable ATP analogs 5'-adenylylimidodiphosphate and adenosine 5'-O-(3-thiotriphosphate) did elicit a significant reduction in GRF binding. The effect of GppNHp was half-maximal at 0.2 μM, and the maximum inhibition achieved was 85%. The effect of 0.1 μM GppNHp on GRF competitive displacement experiments indicated a significant reduction in affinity for the ligand (Kd = 0.51 ± 0.11 nM in the absence of GppNHp and 2.1 ± 1.1 nM in its presence) without an effect on receptor number. The GRF radioligand dissociates slowly from its receptor (t.∧ = 250 ± 50 min), but the addition of 0.1 fiU GppNHp converts approximately half of the receptors present to a more rapidly dissociating form (tA = 9 ± 10 min). These results are consistent with existing models for receptor- G-protein interactions, and thus, we conclude that transduction of the GRF response across the cell membrane involves a guanine nucleotide-binding protein, presumably G8. (Endocrinology124: 24–29, 1989)" @default.
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- W2138777783 date "1989-01-01" @default.
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- W2138777783 title "Nucleotide Regulation of Growth Hormone-Releasing Factor Binding to Rat Pituitary Receptors*" @default.
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- W2138777783 doi "https://doi.org/10.1210/endo-124-1-24" @default.
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