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Conversion of met-enkephalin-Arg6-Phe7 by a purified brain carboxypeptidase (cathepsin A)
| Content Provider | Semantic Scholar |
|---|---|
| Author | Marks, Neville Sachs, Len Stern, Frederic |
| Copyright Year | 1981 |
| Abstract | A carboxypeptidase A-like enzyme known as cathepsin A was purified from rat brain by extraction with Triton X-100, followed by chromatography on DEAE-Sephadex A-50 and gel-filtration. Purified enzyme was devoid of contamination of tryptic-like enzymes, by dipeptidyl carboxypeptidase (angiotensin converting enzyme) and of enkephalinnases cleaving the Tyr-Gly and Gly-Phe bonds of Met-enkephalin. Incubation of purified enzyme with Met-enkephalin-Arg6-Phe7, a naturally occurring enkephalin surrogate, was accompanied by the release of three products as detected by reverse phase HPLC. Subsequent amino acid analysis identified these as Phe, Met-enkephalin-Arg6, and Met-enkephalin, indicating cleavage at the Arg6-Phe7 and Met5-Phe6 bonds. Breakdown followed a precursor-product-relationship with the hexapeptide appearing as an intermediate and the pentapeptide as the final product. The Km for cleavage of the Arg-Phe site was 0.09 mM. Rates of cleavage of hexa- and heptapeptide accord with those found for synthetic N-protected dipeptide substrates. Cathepsin A does not act as an enkephalinase in the accepted sense, since no breakdown of Met-enkephalin was observed. |
| Starting Page | 159 |
| Ending Page | 164 |
| Page Count | 6 |
| File Format | PDF HTM / HTML |
| DOI | 10.1016/S0196-9781(81)80029-0 |
| PubMed reference number | 7291041 |
| Journal | Medline |
| Volume Number | 2 |
| Alternate Webpage(s) | https://api.elsevier.com/content/article/pii/S0196978181800290 |
| Alternate Webpage(s) | https://www.sciencedirect.com/science/article/pii/S0196978181800290?dgcid=api_sd_search-api-endpoint |
| Alternate Webpage(s) | https://doi.org/10.1016/S0196-9781%2881%2980029-0 |
| Journal | Peptides |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
