title: The primary structure of human beta-lipotropin. Further peptide sequencing resolves the controversy and suggests the existence of only one human beta-lipotropin.
abstract: Human beta-lipotropin isolated in Hungary from frozen pituitary glands was purified by high-performance liquid chromatography in Canada. The amino acid sequence of the first 30 residues was determined. Trypsin, trypsin/papain, and trypsin/thermolysin fragments were obtained for the disputed region containing residues 9-25 of beta-lipotropin. Their amino acid composition and sequence established beyond doubt that only one human beta-lipotropin sequence is present. These results suggest the presence of only one gene coding for human pro-opiomelanocortin, the precursor of adrenocorticotropin and beta-endorphin and resolve the controversy over the sequence of human beta-lipotropin.
mesh_terms: D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D010206:Papain / Q000378:metabolism; D010902:Pituitary Gland / Q000032:analysis; D013820:Thermolysin / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism; D008083:beta-Lipotropin / Q000032:analysis*
chemical_list: D008083:beta-Lipotropin; D014357:Trypsin; D010206:Papain; D013820:Thermolysin