Primary structure and morphine-like activity of human beta-endorphin.
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.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001681:Biological Assay; D001921:Brain / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D004723:Endorphins / Q000032:analysis; D006801:Humans; D008297:Male; D051379:Mice; D009020:Morphine; D010446:Peptide Fragments; D010455:Peptides / Q000032:analysis; D051381:Rats; D011957:Receptors, Opioid / Q000378:metabolism; D014649:Vas Deferens / Q000187:drug effects / Q000502:physiology
D000596:Amino Acids; D004723:Endorphins; D010446:Peptide Fragments; D010455:Peptides; D011957:Receptors, Opioid; D009020:Morphine