Recognition of the beta-subunit of human chorionic gonadotropin and sub-determinants by target tissue receptors.
The beta-subunit of human chorionic gonadotropin, purified immunochemically to eliminate undissociated human chorionic gonadotropin, induced testosterone production by mouse Leydig cells at concentrations 400-fold higher than human chorionic gonadotropin. Steroidogenesis was also stimulated by a synthetic fragment of the beta-subunit of human chorionic gonadotropin conforming to the peptide sequence residues 39--71, whereas peptide sequence residues 39--56 and three C-terminal fragments (residues 115--145, 111--145 and 101--145) failed to cause steroidogenesis. These studies suggest the presence in the beta-subunit of human chorionic gonadotropin of determinants recognized by the tissue receptors, a part of these determinants residing between amino acid residues 57--71.
D000818:Animals; D006063:Chorionic Gonadotropin / Q000302:isolation & purification / Q000494:pharmacology*; D066298:In Vitro Techniques; D007985:Leydig Cells / Q000187:drug effects / Q000378:metabolism; D008297:Male; D051379:Mice; D010446:Peptide Fragments / Q000494:pharmacology; D011956:Receptors, Cell Surface / Q000187:drug effects*; D013739:Testosterone / Q000096:biosynthesis
D006063:Chorionic Gonadotropin; D010446:Peptide Fragments; D011956:Receptors, Cell Surface; D013739:Testosterone