Enkephalinases

• Published in: Proceedings of the Royal Society of London. Series B, Biological sciences Biological sciences, 1980-10, Vol.210 (1178), p.123-132
• Main Authors: Gorenstein, C., Snyder, S. H.
• Format: Article
• Language: English
• Subjects: Aminopeptidases - metabolism; Animals; Brain - enzymology; Brain Mapping; Chromatography; Corpus striatum; Electrophoresis; Endorphins - metabolism; Enkephalins - metabolism; Enzymes; Gels; Lectins; Lentils; Male; Molecules; Neurotransmitters; Opioid receptors; Peptide Hydrolases - isolation & purification; Peptide Hydrolases - metabolism; Rats; Substrate Specificity
• ISSN: 0962-8452; 0080-4649; 0950-1193; 1471-2954; 2053-9193
• DOI: 10.1098/rspb.1980.0123

Enkephalins can be degraded by a variety of peptidases. We have characterized several membrane-associated brain peptidases in an effort to determine which if any are concerned with the physiological inactivation of synaptically released enkephalin. We have distinguished two carboxyl-directed dipeptidylpeptidases, designated enkephalinase A$_{1}$ and A$_{2}$, that give rise to the Tyr-Gly-Gly fragment. Both enzymes are physically separable from angiotensin converting enzyme. Regional variations in enkephalinase A$_{1}$ activity and opiate receptors are similar. A novel amino-terminal-directed dipeptidylpeptidase, enkephalinase B, which generates Tyr-Gly, has been identified. All of these enzymes as well as aminopeptidase have been solubilized from brain membranes by detergent treatment and have been mutually resolved by DEAE column chromatography. Enkephalinase A$_{1}$ has been purified 1500-fold, to apparent homogeneity.