Abstract
Enkephalins can be degraded by the 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 A1 and A2, that give rise to the Tyr-Gly-Gly fragment. Both enzymes are physically separable from angiotensin converting enzyme. Regional variations in enkephalinase A1 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 A1 has been purified 1500-fold, to apparent homogeneity.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 123-132 |
| Number of pages | 10 |
| Journal | Proceedings of the Royal Society of London - Biological Sciences |
| Volume | 210 |
| Issue number | 1178 |
| DOIs | |
| State | Published - 1980 |
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology
- General Immunology and Microbiology
- General Environmental Science
- General Agricultural and Biological Sciences