title: Purification and characterization of Atlantic salmon prolactin.
abstract: Prolactin was isolated from the Atlantic salmon (Salmo salar) pituitary gland by extraction with acid acetone, gel filtration, ion exchange-chromatography, and reversed-phase high-performance liquid chromatography. The yield was 0.6 mg/g wet tissue. The hormone had a molecular weight of 23.5 kDa as determined by SDS-polyacrylamide gel electrophoresis. Isoelectric focusing gave an isoelectric point of 9.2. The N-terminal sequence and the amino acid composition indicated extensive homology between Atlantic and Pacific salmon prolactin. Antiserum against Atlantic salmon prolactin cross-reacted with chum salmon prolactin, but not with human, rat, or sheep prolactin.
authors.affiliation: Institute of Medical Biochemistry, University of Oslo, Norway.
authors.forename: O
authors.initials: O
authors.lastname: Andersen
authors.forename: V
authors.initials: V
authors.lastname: Skibeli
authors.forename: K M
authors.initials: KM
authors.lastname: Gautvik
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D005260:Female; D008297:Male; D008969:Molecular Sequence Data; D010903:Pituitary Gland, Anterior / Q000032:analysis*; D011388:Prolactin / Q000032:analysis / Q000302:isolation & purification*; D012474:Salmon / Q000502:physiology*
chemical_list: D000596:Amino Acids; D011388:Prolactin