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Novel opioid peptides derived from casein (beta-casomorphins). II. Structure of active components from bovine casein peptone.
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1979
Year
Pure HeptapeptideMolecular PharmacologyBovine Casein PeptoneActive ComponentsGastrointestinal Peptide HormoneNeuropeptidesBiochemistryMedicineBovine Beta-caseinPeptide TherapeuticPeptide ScienceNon-peptide LigandPharmacologyDrug DiscoveryOpioid Peptides
Material with opioid activity had been isolated from an enzymatic casein digest. It was shown to contain a pure heptapeptide with the sequence Tyr-Pro-Phe-Pro-Gly-Pro-Ile. The identity between the opioid principle and the peptide was proven by the fact that chemical reagents or enzymes effecting one would effect the other. After carboxypeptidase Y digestion a pentapeptide, Tyr-Pro-Phe-Pro-Gly, could be isolated; this peptide showed a higher opioid activity than the heptapeptide. The opioid peptides were highly resistant towards proteolysis, even by pronase. The sequence of the hepatapeptide identified it as a fragment of bovine beta-casein. Therefore it was named beta-casomorphin.