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Functional reconstitution of rat ovarian LH/hCG receptor into proteoliposomes
Author(s) -
Kolena Jaroslav
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80769-0
Subject(s) - receptor , adenylate kinase , cyclase , sodium cholate , gtp' , chemistry , membrane , endocrinology , medicine , biology , biochemistry , enzyme
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 125 I‐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.