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. 1978 Jul;75(7):3153–3157. doi: 10.1073/pnas.75.7.3153

In vitro biosynthesis and chemical characterization of beta-lipotropin, gamma-lipotropin, and beta-endorphin in rat pars intermedia.

N G Seidah, C Gianoulakis, P Crine, M Lis, S Benjannet, R Routhier, M Chrétien
PMCID: PMC392732  PMID: 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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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