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Provedor de dados:  BJMBR
País:  Brazil
Título:  A new brain metalloendopeptidase which degrades the Alzheimer ß-amyloid 1-40 peptide producing soluble fragments without neurotoxic effects
Autores:  Carvalho,K.M.
Data:  1997-10-01
Ano:  1997
Palavras-chave:  Brain metalloendopeptidase
Alzheimer ß-amyloid 1-40 peptide
Alzheimer's disease
Resumo:  A new metalloendopeptidase was purified to apparent homogeneity from a homogenate of normal human brain using successive steps of chromatography on DEAE-Trisacryl, hydroxylapatite and Sephacryl S-200. The purified enzyme cleaved the Gly33-Leu34 bond of the 25-35 neurotoxic sequence of the Alzheimer ß-amyloid 1-40 peptide producing soluble fragments without neurotoxic effects. This enzyme activity was only inhibited by divalent cation chelators such as EDTA, EGTA and o-phenanthroline (1 mM) and was insensitive to phosphoramidon and captopril (1 µM concentration), specific inhibitors of neutral endopeptidase (EC and angiotensin-converting enzyme (EC, respectively. The high affinity of this human brain endopeptidase for ß-amyloid 1-40 peptide (Km = 5 µM) suggests that it may play a physiological role in the degradation of this substance produced by normal cellular metabolism. It may also be hypothesized that the abnormal accumulation of the amyloid ß-protein in Alzheimer's disease may be initiated by a defect or an inactivation of this enzyme.
Tipo:  Info:eu-repo/semantics/article
Idioma:  Inglês
Editor:  Associação Brasileira de Divulgação Científica
Relação:  10.1590/S0100-879X1997001000002
Formato:  text/html
Fonte:  Brazilian Journal of Medical and Biological Research v.30 n.10 1997
Direitos:  info:eu-repo/semantics/openAccess

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