title: Amino acid sequence of growth hormone isolated from medium of incubated pituitary glands of tilapia (Oreochromis mossambicus).
abstract: The amino acid sequence of tilapia (Oreochromis mossambicus) growth hormone (GH) was determined directly by Edman degradation of peptide fragments generated by lysyl endopeptidase and trypsin digestion. The N-terminal residue was deduced to be pyroglutamic acid through the use of pyroglutamyl aminopeptidase; its removal allowed amino acid sequence determination of the remainder of the N-terminal trypsin peptide by Edman degradation. Tilapia GH is composed of 187 amino acid residues and shows high similarity to other perciform GHs. Sequence identities are: 89% with tuna GH, 83% with bonito GH, 85% with yellowtail GH, 89% with red sea bream GH, and 34% with bovine GH. The two asparagine residues (Asn-148 and Asn-184) were recovered by Edman degradation, suggesting the absence of N-glycosylation.
authors.affiliation: Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Japan.
authors.forename: K
authors.initials: K
authors.lastname: Yamaguchi
authors.forename: D S
authors.initials: DS
authors.lastname: King
authors.forename: J L
authors.initials: JL
authors.lastname: Specker
authors.forename: R S
authors.initials: RS
authors.lastname: Nishioka
authors.forename: T
authors.initials: T
authors.lastname: Hirano
authors.forename: H A
authors.initials: HA
authors.lastname: Bern
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D005399:Fishes / Q000378:metabolism*; D013006:Growth Hormone / Q000737:chemistry* / Q000302:isolation & purification; D066298:In Vitro Techniques; D008745:Methylation; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010902:Pituitary Gland / Q000737:chemistry*; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases; D014357:Trypsin
chemical_list: D010446:Peptide Fragments; D013006:Growth Hormone; D012697:Serine Endopeptidases; D014357:Trypsin; C036813:lysyl endopeptidase