Data/hora: 06/06/2024 03:31:43

Provedor de dados: | 56
País: | Brazil
Título: | A liver metalloendopeptidase which degrades the circulating hypotensive peptide hormones bradykinin and atrial natriuretic peptide
Autores: | Carvalho,K.M.; Nava,R.A.; França,M.S.F.; Medeiros,M.A.S.; Camarão,G.C.; Juliano,L.
Data: | 1999-01-01
Ano: | 1999
Palavras-chave: | Liver metalloendopeptidase; Bradykinin; Atrial natriuretic peptide.
Resumo: | A new metalloendopeptidase was purified to apparent homogeneity from a homogenate of normal human liver using successive steps of chromatography on DEAE-cellulose, hydroxyapatite and Sephacryl S-200. The purified enzyme hydrolyzed the Pro7-Phe8 bond of bradykinin and the Ser25-Tyr26 bond of atrial natriuretic peptide. No cleavage was produced in other peptide hormones such as vasopressin, oxytocin or Met- and Leu-enkephalin. This enzyme activity was inhibited by 1 mM divalent cation chelators such as EDTA, EGTA and o-phenanthroline and was insensitive to 1 µM phosphoramidon and captopril, specific inhibitors of neutral endopeptidase (EC 3.4.24.11) and angiotensin-converting enzyme (EC 3.4.15.1), respectively. With Mr 85 kDa, the enzyme exhibits optimal activity at pH 7.5. The high affinity of this endopeptidase for bradykinin (Km = 10 µM) and for atrial natriuretic peptide (Km = 5 µM) suggests that it may play a physiological role in the inactivation of these circulating hypotensive peptide hormones.
Tipo: | Info:eu-repo/semantics/other
Idioma: | Inglês
Identificador: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000100007
Editor: | Associação Brasileira de Divulgação Científica
Relação: | 10.1590/S0100-879X1999000100007
Formato: | text/html
Fonte: | Brazilian Journal of Medical and Biological Research  v.32 n.1 1999
Fonte: | info:eu-repo/semantics/openAccess