Opioid Peptides and Protein Phosphorylation

  • Leonard G. Davis
  • Yigal H. Ehrlich
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 116)


The identification and isolation of naturally occur ring neuropeptides with morDhine-like activity was first reported by Hughes (1975) and co-workers (HUGHES, et al, 1975). These compounds were named methionine-enkephalin and leucine-enkephalin and have the amino-acid sequences of Tyr-Gly-Gly-Phe-Met and Tyr-Gly-Gly-Phe-Leu, respectively. Subsequently, a 31 amino-acid peptide with similar pharmacological and biochemical properties was described (COX, et al, 1975; BRADBURv, et al, 1976; GUILLEMAN, et al, 1976). Sequential amino-acid analysis of this larger peptide, named ß-endorphin, demonstrated a similarity to the C-terminal portion (#61-91) in the sequence of ß-lipotropin (LI and CHUNG, 1976: see Figure 1). Using the mouse vas deferens, the guinea pig ileum, or the opiate receptor assays, it was shown that these neuropeptides act in vitro similar to alkaloid opiates like morphine (HUGHES, 1975; HUGHES, et al, 1975; LI and CHUNG, 1976; SIMANTOV and SNYDER, 1976; GRAF, et al, 1976). These endogenous opioidlike neuropeptides have been shown to interact differentially with the opiate receptors of brain (LORD, et al, 1976).


Protein Phosphorylation Opioid Peptide Opiate Receptor Phosphorylative Activity Phosphorylation Assay 
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Copyright information

© Plenum Press, New York 1979

Authors and Affiliations

  • Leonard G. Davis
    • 1
  • Yigal H. Ehrlich
    • 1
  1. 1.Missouri Institute of Psychiatry, School of MedicineUniversity of Missouri-ColumbiaSt. LouisUSA

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