title: Purification and properties of choriogonadotropin from human term placenta.
abstract: Affinity chromatography has been applied successfully to the isolation of human choriogonadotropin from human term placenta. In a single step, a 57-fold purification was achieved. Evidence is presented which indicates that the product contains intact hormone as well as its free alpha-subunit. Preliminary data suggest that a variant form of alpha-subunit is also present which has serine as its N-terminal and contains relatively little arginine and proline as compared to the authentic alpha-subunit.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D006063:Chorionic Gonadotropin / Q000302:isolation & purification; D002846:Chromatography, Affinity; D005260:Female; D006801:Humans; D007118:Immunoassay; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis; D010920:Placenta / Q000032:analysis*; D011247:Pregnancy
chemical_list: D000596:Amino Acids; D006063:Chorionic Gonadotropin; D046911:Macromolecular Substances; D010446:Peptide Fragments