| Registro completo |
| Provedor de dados: |
BJMBR
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| País: |
Brazil
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| Título: |
A liver metalloendopeptidase which degrades the circulating hypotensive peptide hormones bradykinin and atrial natriuretic peptide
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| Autores: |
Carvalho,K.M.
Nava,R.A.
França,M.S.F.
Medeiros,M.A.S.
Camarão,G.C.
Juliano,L.
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| Data: |
1999-01-01
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| Ano: |
1999
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| Palavras-chave: |
Liver metalloendopeptidase
Bradykinin
Atrial natriuretic peptide
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| 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.
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| Tipo: |
Info:eu-repo/semantics/other
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| Idioma: |
Inglês
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| Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000100007
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| Editor: |
Associação Brasileira de Divulgação Científica
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| Relação: |
10.1590/S0100-879X1999000100007
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| Formato: |
text/html
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| Fonte: |
Brazilian Journal of Medical and Biological Research v.32 n.1 1999
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| Direitos: |
info:eu-repo/semantics/openAccess
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