title: N-terminal amino-sequencing of camel (Camelus dromedarius) luteinizing-hormone alpha and beta-subunits.
abstract: The subunits of luteinizing hormone from the Camelus dromedarius (CamLH) have been separated by reverse phase HPLC after reduction and alkylation of their disulfide bridges. The N-terminal amino-acid sequencing of the alpha and beta subunits has been performed up to the 53rd and 67th residue respectively (i.e. more than half of each polypeptide chain). These sequences have been compared to those of LH from other mammalian species in order to estimate the phylogenetic divergence of LH in this species and in order to point out characteristic features of its primary structure that can be related to its physico-chemical properties.
authors: Unité Endocrinologie de la Gamètogenèse, Institut National de la Recherche Agronomique, URA CNRS 234, Nouzilly, France.
authors: Y
authors: Y
authors: Combarnous
authors: J C
authors: JC
authors: Huet
authors: N
authors: N
authors: Martinat
authors: M
authors: M
authors: Mansion
authors: A
authors: A
authors: Anouassi
authors: J C
authors: JC
authors: Pernollet
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002162:Camelus; D002851:Chromatography, High Pressure Liquid; D015292:Glycoprotein Hormones, alpha Subunit / Q000302:isolation & purification; D006801:Humans; D007986:Luteinizing Hormone / Q000302:isolation & purification; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid
chemical_list: D015292:Glycoprotein Hormones, alpha Subunit; D007986:Luteinizing Hormone