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| Medeiros,M.A.S.; França,M.S.F.; Boileau,G.; Juliano,L.; Carvalho,K.M.. |
| Two intramolecularly quenched fluorogenic peptides containing o-aminobenzoyl (Abz) and ethylenediamine 2,4-dinitrophenyl (EDDnp) groups at amino- and carboxyl-terminal amino acid residues, Abz-<!-- $MVD$:face("Times") -->DArg-Arg-Leu-EDDnp (Abz-<!-- $MVD$:face("Times") -->DRRL-EDDnp) and Abz-<!-- $MVD$:face("Times") -->DArg-Arg-Phe-EDDnp (Abz-<!-- $MVD$:face("Times") -->DRRF-EDDnp), were selectively hydrolyzed by neutral endopeptidase (NEP, enkephalinase, neprilysin, EC 3.4.24.11) at the Arg-Leu and Arg-Phe bonds, respectively. The kinetic parameters for the NEP-catalyzed hydrolysis of Abz-<!-- $MVD$:face("Times") -->DRRL-EDDnp and Abz-<!-- $MVD$:face("Times") -->DRRF-EDDnp were Km = 2.8 µM, kcat = 5.3 min-1, kcat/Km = 2... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Neutral endopeptidase; Enkephalinase; Neprilysin; Fluorogenic substrates; Phosphoramidon. |
| Ano: 1997 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997001000003 |
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| Carvalho,K.M.; Nava,R.A.; França,M.S.F.; Medeiros,M.A.S.; Camarão,G.C.; Juliano,L.. |
| 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... |
| Tipo: Info:eu-repo/semantics/other |
Palavras-chave: Liver metalloendopeptidase; Bradykinin; Atrial natriuretic peptide. |
| Ano: 1999 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000100007 |
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