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Primary structure and morphine-like activity of human beta-endorphin.

UniProtKB (1) rdf/xml

Dragon N., Seidah N.G., Lis M., Routhier R., Chretien M.

The complete amino acid sequence of human beta-endorphin was obtained by automatic sequencing of a sulfonyl isothiocyanate derivative of this peptide, in combination with peptide mapping of a tryptic digest of the native molecule. It was found to be identical with the carboxy-terminal portion 61-91 of human beta-lipotropin (beta-LPH). The morphine-like activity of beta-endorphin is comparable both in the mouse vas deferens bioassay and in the opiate receptor binding assay. However, beta-LPH is not active up to concentrations of 10(-6) M.

Can. J. Biochem. 55:666-670(1977) [PubMed] [Europe PMC]