title: Isolation and characterization of growth hormone from Atlantic cod (Gadus morhua).
abstract: Growth hormone was purified from cod pituitary extract by a simple two-step procedure involving gel filtration and reversed-phase high-performance liquid chromatography (rpHPLC). At each stage of purification, fractions were monitored by rpHPLC, SDS-polyacrylamide gel electrophoresis, and immunoblotting using anti-chum salmon growth hormone (GH) antiserum. The yield of purified hormone was 1.3 mg/g pituitary. Cod GH was found to exist in two monomeric forms (Mr = 20K and 22K) and dimeric forms (Mr = 40K and 42K). The two monomeric forms have a pI of 5.8, an identical amino acid composition, histidine as the N-terminal residue, and an identical lysyl endopeptidase peptide map. Staining with concanavalin A was observed on the 20K component only, but analysis for total reducing sugar did not confirm these results. Cod GH was found to be a potent stimulator of growth in juvenile rainbow trout which received intraperitoneal injections of the hormone. The partial amino acid sequence has been determined.
authors.affiliation: Department of Biochemistry, University of Bergen, Bergen, Norway.
authors.forename: M
authors.initials: M
authors.lastname: Rand-Weaver
authors.forename: B T
authors.initials: BT
authors.lastname: Walther
authors.forename: H
authors.initials: H
authors.lastname: Kawauchi
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003208:Concanavalin A; D005399:Fishes / Q000378:metabolism*; D013006:Growth Hormone / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D015151:Immunoblotting; D008969:Molecular Sequence Data
chemical_list: D003208:Concanavalin A; D013006:Growth Hormone