Functional reconstitution of rat ovarian LH/hCG receptor into proteoliposomes

Rat ovarian membrane LH/hCG receptor was solubilized in various detergents and reconstituted into proteoliposomes. Upon removal of sodium cholate by active absorption on Bio-Beads SM-2, the functional interaction between receptor and adenylate cyclase was restored. Adenylate cyclase was stimulated b...

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Bibliographic Details
Published in:FEBS letters 1989-07, Vol.250 (2), p.425-428
Main Author: Kolena, Jaroslav
Format: Article
Language:English
Subjects:
Adenylate cyclase
Adenylyl Cyclases - metabolism
Animals
Biological and medical sciences
Cell receptors
Cell structures and functions
Female
Fundamental and applied biological sciences. Psychology
Hormone receptor
Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors
liposomes
Molecular and cellular biology
Ovary - enzymology
Ovary - metabolism
Proteolipids - metabolism
Rat ovary
Rats
Rats, Inbred Strains
Receptors, Gonadotropin - metabolism
Receptors, LH - metabolism
Reconstitution
Sodium cholate
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Summary:Rat ovarian membrane LH/hCG receptor was solubilized in various detergents and reconstituted into proteoliposomes. Upon removal of sodium cholate by active absorption on Bio-Beads SM-2, the functional interaction between receptor and adenylate cyclase was restored. Adenylate cyclase was stimulated by hCG, HCG+GTP or GppNHp and NaF. Reconstituted proteoliposomes bound more 125I-hCG (528 fmol/mg protein) than membrane-bound receptors (384 fmol/mg protein). There was no difference, however, in the relative affinity of reconstituted receptor preparations for hCG.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(89)80769-0