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

Article Details

Citation

Dragon N, Seidah NG, Lis M, Routhier R, Chretien M

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

Can J Biochem. 1977 Jun;55(6):666-70.

PubMed ID
195688 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Pro-opiomelanocortinP01189Details