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Cleavage of atrial natriuretic peptide by a kidney membrane-bound carboxypeptidase A

par Michel, Alain ;Nortier, Joëlle ;Humblet, Anne;Paradis, Caroline;De Prez, Eric ;Deschodt Lanckman, Monique
Référence Peptides, 19, page (907-912)
Publication Publié, 1998

Article révisé par les pairs

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Résumé :

An enzymatic activity that cleaved the C-terminal Tyr of ANP (1-28) was characterized in human kidney microvillar membranes by using 125I-labeled rat ANP as substrate. This activity was inhibited by potato carboxypeptidase inhibitor (PCI) and 1,10 phenanthroline, suggesting that it corresponded to a metallocarboxypeptidase. Solubilization experiments indicated that the carboxypeptidase activity could be recovered in the supernatant after 1% Triton X-100 extraction. As separation by ion exchange chromatography revealed several peaks of enzyme activity, PCI coupled to Sepharose was used for purification. This step resulted in a single protein band at 30 kDa, as analyzed by SDS-PAGE.