Localization and characterization of aminopeptidase P in bovine adrenal medulla. |
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| Authors: | G Vanhoof J De Block I De Meester S Scharpé W P De Potter |
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| Affiliation: | Laboratory of Clinical Biochemistry, University of Antwerp, Wilrijk, Belgium. |
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| Abstract: | Aminopeptidase P (EC 3.4.11.9) is demonstrated for the first time in the cytosolic fraction of chromaffin cells of the bovine adrenal medulla. The enzyme is inhibited by metal chelators and by sulfhydryl-reactive agents, which suggests that both a tightly bound metal ion and a cysteine residue are necessary for enzymatic activity. Aminopeptidase P might be important for the modulation of the biological activity of neuropeptides. Its occurrence in the adrenal chromaffin cells provides a useful tool for studying the function of this unique proline-specific peptidase in neuropeptide processing and secretion. |
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