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

ABSTRACT 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 > 70%) of the LHRH-...

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Published inJournal of endocrinology Vol. 115; no. 1; pp. 151 - 159
Main Authors OGIER, S.-A, MITCHELL, R, FINK, G
Format Journal Article
LanguageEnglish
Published Colchester BioScientifica 01.10.1987
Portland Press
Subjects
Animals
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Gonadotropin-Releasing Hormone
Hormones and neuropeptides. Regulation
Hypothalamus. Hypophysis. Epiphysis. Urophysis
luteinizing hormone-releasing hormone
Male
Methods
Molecular Weight
pituitary (anterior)
Pituitary Gland, Anterior - analysis
Rats
Rats, Inbred Strains
Receptors, Cell Surface - analysis
Solubility
solubilization
Vertebrates: endocrinology
Adenohypophysis
Vertebrata
Membrane receptor
Mammalia
Rat
Gonadotropic cell
Rodentia
Peptide hormone
Gonadotropin RH
Solubilization
Hormonal receptor
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Summary:ABSTRACT 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 > 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. J. Endocr. (1987) 115, 151–159
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0022-0795
1479-6805
DOI:10.1677/joe.0.1150151