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A new fluorometric assay for neutral endopeptidase (EC 3.4.24.11)
Braz. j. med. biol. res ; 28(10): 1055-9, Oct. 1995. graf
Artigo em Inglês | LILACS | ID: lil-160995
ABSTRACT
An intramolecularly quenched fluorogenic peptide structurally related to Leu-enkephalin, Abz-GGdFLRRV-EDDnp, was selectively hydrolyzed at the R-V bond by neutral endopeptidase (NEP, enkephalinase, neprilysin, EC 3.4.24.11) with kinetic parameters (Km = 3 µM,Kcat = 127 / min and Kcat / Km = 42 / min µM) similar to those of Leu-enkephalin. The specificity of the assay for NEP was demostrated by incubating Abz-GGdFLRRV-EDDnp with a kidney homogenate and with crude membrane preparations of brain and lung. For all three homogenates the complementary fragments Abz-GGdFLRRnp accounted for more than 95 percent of the products wich were totally inhibited by 1 µM thiorphan, a highly specific NEP inhibitor. A continuous fluorometric assay for only 5 min was sufficient to quantify the NEP activity with a minimum sensitivity of 5 ng of purified NEP or the equivalent enzymatic activity in crude tissue preparations.
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Índice: LILACS (Américas) Assunto principal: Neuropeptídeos / Neprilisina Limite: Animais Idioma: Inglês Revista: Braz. j. med. biol. res Assunto da revista: Biologia / Medicina Ano de publicação: 1995 Tipo de documento: Artigo / Congresso e conferência

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Índice: LILACS (Américas) Assunto principal: Neuropeptídeos / Neprilisina Limite: Animais Idioma: Inglês Revista: Braz. j. med. biol. res Assunto da revista: Biologia / Medicina Ano de publicação: 1995 Tipo de documento: Artigo / Congresso e conferência