title: [Important role of C-terminal amino acid sequence of the luteinizing hormone alpha-subunit in its recombination with the beta-subunit].
abstract: Five amino acid residues, i. e. serine, lysine, histidine and two tyrosine residues, are split from the C-end of the alpha-subunit of bovine luteinizing hormone by carboxypeptidase A. Gel-filtration through Sephadex G-100 demonstrated that the carboxypeptidase-treated alpha-subunit is not recombined with the native beta-subunit and does not form complex molecules of the hormone.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002268:Carboxypeptidases / Q000378:metabolism; D002417:Cattle; D002850:Chromatography, Gel; D006639:Histidine / Q000378:metabolism; D007986:Luteinizing Hormone / Q000032:analysis*; D008239:Lysine / Q000378:metabolism; D012694:Serine / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism
chemical_list: D014443:Tyrosine; D012694:Serine; D006639:Histidine; D007986:Luteinizing Hormone; D002268:Carboxypeptidases; D008239:Lysine
vernacular_title: Vazhnaia rol' C-kontsevoĭ aminokislotnoĭ posledovatel'nosti alpha-sub'edinitsy liuteiniziruiushchego gormona pri ee rekombinatsii s beta-sub'edinitseĭ