Enkephalinase: selective inhibitors and partial characterization. Academic Article uri icon

Overview

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 dependence, for activity in several buffers and for susceptibility to specific inhibitors.

publication date

  • January 1, 1980

Research

keywords

  • Caudate Nucleus
  • Endorphins
  • Enkephalins
  • Oligopeptides
  • Protease Inhibitors

Identity

Scopus Document Identifier

  • 0019126290

Digital Object Identifier (DOI)

  • 10.1016/0196-9781(80)90032-7

PubMed ID

  • 6264406

Additional Document Info

volume

  • 1

issue

  • 1