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 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.
Kolena
J
J
Institute of Experimental Endocrinology, Slovak Academy of Sciences, Bratislava.
D000262:Adenylyl Cyclases / Q000378:metabolism; D000818:Animals; D005260:Female; D010053:Ovary / Q000201:enzymology / Q000378:metabolism*; D011510:Proteolipids / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D011967:Receptors, Gonadotropin / Q000378:metabolism*; D011974:Receptors, LH / Q000378:metabolism*
D011510:Proteolipids; D011967:Receptors, Gonadotropin; D011974:Receptors, LH; D000262:Adenylyl Cyclases