Degradation of α and β neo-endorphin by rat brain membrane peptidases

Charles Ulrich, Louis B. Hersh

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


Fractionation of Triton-solubilized rat brain membranes on diethylaminoethyl-cellulose resolves two peptidases which hydrolyze β-neo-endorphin. One of these peptidases was identified as Angiotensin Converting Enzyme by (a) its sensitivity to inhibition by the specific inhibitors MK422 and captopril, (b) by the identification of reaction products, and (c) by comparison to authentic angiotensin converting enzyme. In contrast, α-neo-endorphin hydrolysis by angiotensin converting enzyme could not be detected. The second enzyme active on β-neo-endorphin was identified as an aminopeptidase. This aminopeptidase is identical to the previously described enkephalin-degrading aminopeptidase. The possible involvement of these enzymes in the metabolism of opioid peptides is discussed.

Original languageEnglish
Pages (from-to)475-482
Number of pages8
Issue number3
StatePublished - 1985

Bibliographical note

Funding Information:
The technical assistance of Ms. Vicki Choate is gratefully acknowledged. Charles Ulrich is a recipient of a Chilton Foundation fellowship. This research was supported in part by Grant No. DA-02243 from N1DA and Grant No. 1-131 from the Robert A. Welch Foundation, Houston, Texas.


  • Aminopeptidase
  • Angiotensin converting enzyme
  • Neo-endorphins
  • Opioid peptide degradation

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience


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