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  • Title: In vitro biosynthesis and chemical characterization of beta-lipotropin, gamma-lipotropin, and beta-endorphin in rat pars intermedia.
    Author: Seidah NG, Gianoulakis C, Crine P, Lis M, Benjannet S, Routhier R, Chrétien M.
    Journal: Proc Natl Acad Sci U S A; 1978 Jul; 75(7):3153-7. PubMed ID: 277917.
    Abstract:
    Three 3-hr incubations of pars intermedia cells from 40 rat pituitaries with [35S]methionine, [3H]lysine, and [3H]leucine sufficed for the identification and chemical characterization of biosynthesized beta-lipotropin, gamma-lipotropin, and beta-endorphin. From the molecular weight, migration on polyacrylamide gels, and sequence Met5, Lys9, Leu14,17, rat beta-endorphin was shown to be identical to its sheep homologue and no trace of Leu5 beta-endorphin could be detected. Rat beta-lipotropin differs from that of sheep in its elution properties on CM-cellulose, and its sequence shows Leu2,10,14, Lys20. Rat gamma-lipotropin shows the same NH2-terminal sequence as beta-lipotropin and is again different from its sheep homologue. The identification of rat beta-lipotropin was confirmed by its selective cleavage into beta-endorphin after trypsin digestion of the citraconylated peptide, a property not observed with rat gamma-lipotropin.
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