Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/26555
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dc.contributor.authorOliveira, V
dc.contributor.authorCampos, M.
dc.contributor.authorHemerly, J. P.
dc.contributor.authorFerro, E. S.
dc.contributor.authorCamargo, ACM
dc.contributor.authorJuliano, M. A.
dc.contributor.authorJuliano, L.
dc.date.accessioned2016-01-24T12:31:23Z-
dc.date.available2016-01-24T12:31:23Z-
dc.date.issued2001-05-15
dc.identifierhttp://dx.doi.org/10.1006/abio.2001.5083
dc.identifier.citationAnalytical Biochemistry. San Diego: Academic Press Inc Elsevier Science, v. 292, n. 2, p. 257-265, 2001.
dc.identifier.issn0003-2697
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/26555-
dc.description.abstractInternally quenched fluorescent peptides derived from neurotensin (pELYENKPRRPYIL) sequence were synthesized and assayed as substrates for neurolysin (EC 3.4.24.16), thimet oligopeptidase (EC 3.4.24.15 or TOP), and neprilysin (EC 3.4.24.11 or NEP), Abz-LYENKPRRPYILQ-EDDnp (where EDDnp is N-(2,4-dinitrophenyl)ethylenediamine and Abz is ortho-aminobenzoic acid) was derived from neurotensin by the introduction of Q-EDDnp at the C-terminal end of peptide and by the substitution of the pyroglutamic (pE) residue at N-terminus for Abz and a series of shorter peptides was obtained by deletion of amino acids residues from C-terminal, N-terminal, or both sides. Neurolysin and TOP hydrolyzed the substrates at P-Y or Y-I or R-R bonds: depending on the sequence and size of the peptides, while NEP cleaved P-Y or Y-I bonds according to its S'(1) specificity. One of these substrates, Abz-NKPRRPQ-EDDnp was a specific and sensitive substrate for neurolysin (k(cat) = 7.0 s(-l), K(m) = 1.19 muM and k(cat)/K(m) = 5882 mM-(1) . s-(1)), while it was completely resistant to NEP and poorly hydrolyzed by TOP and also by prolyl oligopeptidase (EC 3.4.21.26), Neurolysin concentrations as low as 1 pM were detected using this substrate under our conditions and its analogue Abz-NKPRAPQ-EDDnp was hydrolyzed by neurolysin with k(cat) = 14.03 s(-1), K(m) = 0.82 muM, and k(cat)/K(m) = 17,110 mM(-1) . s(-1), being the best substrate so far described for this peptidase. (C) 2001 Academic Press.en
dc.format.extent257-265
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofAnalytical Biochemistry
dc.rightsAcesso restrito
dc.subjectfluorogenic substratesen
dc.subjectneurotensinen
dc.subjectneurolysinen
dc.subjectthimet oligopeptidaseen
dc.subjectneprilysinen
dc.subjectprolyl oligopeptidaseen
dc.titleSelective neurotensin-derived internally quenched fluorogenic substrates for neurolysin (EC 3.4.24.16): Comparison with thimet oligopeptidase (EC 3.4.24.15) and neprilysin (EC 3.4.24.11)en
dc.typeArtigo
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionInst Butantan
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Inst Biomed Sci, Dept Histol, BR-05508900 São Paulo, Brazil
dc.description.affiliationInst Butantan, Biochem & Biophys Lab, BR-05503900 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.identifier.doi10.1006/abio.2001.5083
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000168902300012
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