Evidence for Sex Differences in GnRH Receptors and Mechanism of Action

Mitchell, R. M.; Ogier, Sally-Ann; Johnson, Mark; Cleland, A.; Bennie, J.; Fink, George

doi:10.1007/978-1-4684-5131-3_9

Cited by 2 publications

(1 citation statement)

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“…Equilibrium binding assay Standard equilibrium binding assays were carried out with the protected LHRH analogue buserelin (dSer(Bu')6 des Gly10 LHRH-ethylamide; a generous gift from Hoechst A.G., Frankfurt, F.R.G), which was iodinated with 125I to a specific activity of about 1100 Ci/mmol by the chloramine method (Mitchell, Ogier, Johnson et al 1985). Luteinizing hormonereleasing hormone and its analogues [des pGlu1]-LHRH and [D-pGlu1,D-Phe2,D-Trp36]-LHRH were obtained from Sigma.…”

Section: Receptor Solubilizationmentioning

confidence: 99%

Solubilization of a large molecular weight form of the rat LHRH receptor

Ogier

Mitchell²,

Fink³

1987

Journal of Endocrinology

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The LHRH receptor has been solubilized from male rat anterior pituitary glands, using the zwitterionic detergent 3-((3-cholamidopropyl)-dimethylammonio)-1-propanesulphonate in the presence of a high concentration of sodium chloride. This method gave high yields (up to greater than 70%) of the LHRH-binding site from the membrane preparation. Ligand binding studies using LHRH analogues were carried out to determine dissociation constants for LHRH receptors both in situ in the membrane preparation and for solubilized LHRH receptors. For all the analogues the binding characteristics were similar in both preparations, suggesting that the solubilization procedure left the LHRH receptor undenatured. Gel filtration revealed an apparent molecular weight for the LHRH receptor of 100,000-160,000, with the mean value being approximately twice that found by others using sodium dodecyl sulphate-polyacrylamide gel electrophoretic techniques. The results indicate that the LHRH receptor probably exists in gonadotroph membranes as a large complex of more than one subunit.

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Section: Receptor Solubilizationmentioning

confidence: 99%