| Autor: |
Toll L; Life Sciences Division, SRI International, Menlo Park, CA 94025., Brandt SR, Olsen CM, Judd AK, Almquist RG |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1991 Mar 29; Vol. 175 (3), pp. 886-93. |
| DOI: |
10.1016/0006-291x(91)91648-v |
| Abstrakt: |
An endopeptidase isolated from bovine kidney displays high affinity and selectivity for the Ser-Phe bond located in the C-terminal region of atrial peptides. Enzymatic activity converts APIII and APII to the less active peptide API. This peptidase is inhibited by both metal chelators and sulfhydryl-reactive agents, suggesting both a tightly bound metal and a cysteine residue are important for enzymatic activity. This enzyme may be important for the processing and/or degradation of atrial peptides. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
