Enkephalinase: Selective inhibitors and partial characterization

Sue Sullivan, Huda Akil, Deborah Blacker, Jack D. Barchas

Research output: Contribution to journalArticlepeer-review

35 Scopus citations

Abstract

There are at least two types of enzymes in brain, endopeptidases and aminopeptidases, which metabolize enkephalins. Evidence is presented to suggest that enkephalinase, an endopeptidase cleaving at the Gly-Phe bond, is specific for the endogenous enkephalinergic system. Selective inhibitors are described for each enzyme. These are parachloromercuriphenylsulfonic acid and puromycin in the case of aminopeptidases and various enkephalin fragments in the case of enkephalinase. Some characteristics of the two types of enzymes are described. Enkephalinase has many properties in common with the well-characterized brain angiotensin-converting enzyme. These two enzymes, however, behaved differently when tested for chloride dependance, for activity in several buffers and for susceptibility to specific inhibitors.

Original languageEnglish
Pages (from-to)31-35
Number of pages5
JournalPeptides
Volume1
Issue number1
DOIs
StatePublished - 1980
Externally publishedYes

Keywords

  • Aminopeptidase metabolism of enkephalin
  • Enkephalin degradation
  • Enkephalinase and angiotensin converting enzyme
  • Enkephalinase inhibitors
  • Enkephalinase properties

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