Abstract
The cytosolic dipeptidyl-aminopeptidase III (EC 3.4.14.4) from rat brain was partially purified using Arg-Arg-4-methoxy-β-naphthylamide as a substrate. It was completely separated from aminopeptidase B on DEAE-Sephacel ion exchange chromatography. Similar to bovine pituitary dipeptidyl-aminopeptidase III, it has a pH optimum of 9, prefers Arg-Arg-4-methoxy-β-naphthylamide as a substrate, and catalyzes the sequential release of dipeptides from the NH2 terminus of peptide substrates provided they are not smaller than a tetrapeptide. Among numerous biologically active peptides tested, angiotensins and enkephalins were the most preferred substrates with micromolar affinities, suggesting that dipeptidyl-aminopeptidase III may play a physiologic role in regulating enkephalin and/or angiotensin disposition.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 12043-12050 |
| Number of pages | 8 |
| Journal | Journal of Biological Chemistry |
| Volume | 257 |
| Issue number | 20 |
| State | Published - 1982 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology