Characterization of four substrates emphasizes kinetic similarity between insect and human C-domain angiotensin-converting enzyme

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dc.contributor.authorHens, K.
dc.contributor.authorVandingenen, A.
dc.contributor.authorMacours, N.
dc.contributor.authorBaggerman, G.
dc.contributor.authorCarmona, Adriana Karaoglanovic [UNIFESP]
dc.contributor.authorSchoofs, L.
dc.contributor.authorDe Loof, A.
dc.contributor.authorHuybrechts, R.
dc.contributor.institutionCatholic Univ Louvain
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T12:33:26Z
dc.date.available2016-01-24T12:33:26Z
dc.date.issued2002-07-01
dc.description.abstractAngiotensin converting enzyme (ACE) was already discovered in insects in 1994, but its physiological role is still enigmatic. We have addressed this problem by purifying four new ACE substrates from the ovaries of the grey fleshfly, Neobellieria bullata . Their primary structures were identified as NKLKPSQWISLSD (Neb -ODAIF- 1(1-13) ), NKLKPSQWI (Neb -ODAIF- 1(1-9) ), SLKPSNWLTPSE (Neb -ODAIF- 2) and LEQIYHL. Database analysis showed significant homology with amino acid sequence stretches as present in the N-terminal part of several fly yolk proteins. An antiserum raised against Neb -ODAIF-1(1-9) immunostained one out of three yolk protein bands of SDS/PAGE-separated fly haemolymph and egg homogenate, thus confirming that these peptides originate from a yolk protein gene product. Kinetic analysis of these peptides and of the peptides Neb -ODAIF and Neb -ODAIF- 1(1-7) with insect ACE and human ACE show both similar and unique properties for insect ACE as compared with human C-domain ACE.en
dc.description.affiliationCatholic Univ Louvain, Inst Zool, Lab Dev Physiol & Mol Biol, B-3000 Louvain, Belgium
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent3522-3530
dc.identifierhttp://dx.doi.org/10.1046/j.1432-1033.2002.03043.x
dc.identifier.citationEuropean Journal of Biochemistry. Oxford: Blackwell Publishing Ltd, v. 269, n. 14, p. 3522-3530, 2002.
dc.identifier.doi10.1046/j.1432-1033.2002.03043.x
dc.identifier.issn0014-2956
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/26901
dc.identifier.wosWOS:000176920600021
dc.language.isoeng
dc.publisherBlackwell Publishing Ltd
dc.relation.ispartofEuropean Journal of Biochemistry
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectACE kineticsen
dc.subjectdomain specific substratesen
dc.subjectinsect physiologyen
dc.subjectreproductionen
dc.titleCharacterization of four substrates emphasizes kinetic similarity between insect and human C-domain angiotensin-converting enzymeen
dc.typeinfo:eu-repo/semantics/article
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