Canadian Journal of Biochemistry · 1977 · 21 citations · 0 references
MedicineEndocrinologyPharmacologyBiochemical PharmacologyHormone BiochemistryNeuropharmacologyAnalgesic PharmacologyOpioid AnalgesicsOpioid PharmacologyPeptide ChemistryPeptide Hormone BiochemistryReceptor PharmacologyAmino Acid Sequence-structure RelationshipsHormone Primary StructureOpioid Peptide PharmacologyOpioid Receptor BindingPeptide Hormone PharmacologyPeptide Hormone ReceptorsPeptide MappingPeptide-to-protein Mapping
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.