title: Primary structure of fox pituitary growth hormone.
abstract: Tryptic digests of fox growth hormone (fGH) were separated by reverse phase high performance liquid chromatography (HPLC) and by paper electrophoresis. From the amino acid composition of these tryptic peptides and from their alignment with the expected tryptic peptides from bovine growth hormone (bGH), the primary structure of fGH is proposed. There are only 17 amino acid residues which are different in these two growth hormone molecules.
authors.affiliation: Laboratory of Molecular Endocrinology, University of California, San Francisco.
authors.forename: C H
authors.initials: CH
authors.lastname: Li
authors.forename: J
authors.initials: J
authors.lastname: Izdebski
authors.forename: D
authors.initials: D
authors.lastname: Chung
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D005589:Foxes / Q000378:metabolism*; D013006:Growth Hormone / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010902:Pituitary Gland / Q000378:metabolism; D014357:Trypsin
chemical_list: D010446:Peptide Fragments; D013006:Growth Hormone; D014357:Trypsin