Determination of angiotensin I-converting enzyme activity in equine blood: lack of agreement between methods of analysis

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dc.contributor.authorCosta, Maria Fernanda de Mello
dc.contributor.authorCarmona, Adriana Karaoglanovic [UNIFESP]
dc.contributor.authorAlves, Marcio Fernando Madureira [UNIFESP]
dc.contributor.authorRyan, Timothy M.
dc.contributor.authorDavies, Helen M.
dc.contributor.authorAnderson, Garry A.
dc.contributor.authorSlocombe, Ron F.
dc.contributor.institutionUniv Melbourne
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T14:06:14Z
dc.date.available2016-01-24T14:06:14Z
dc.date.issued2011-03-01
dc.description.abstractAngiotensin-I converting enzyme (ACE) is a key regulator of blood pressure, electrolytes and fluid homeostasis through conversion of angiotensin I into angiotensin II. Recently, a genetic polymorphism of the ACE gene, which accounts for 47% of the variation of ACE activity in blood, has been advocated as a biomarker of athletic aptitude. Different methods of analysis and determination of ACE activity in plasma have been used in human and equine research without a consensus of a gold standard method. Different methods have often been used interchangeably or cited as being comparable in the existing literature; however, the actual agreement between assays has not been investigated. Therefore, in this study, we evaluated the level of agreement between three different assays using equine plasma obtained from 29 horses. Two spectrophotometric assays using Furylacryloyl-phenylalanyl-glycyl-glycine as substrate and one fluorimetric assay utilizing o-aminobenzoic acid-FRK-(Dnp)P-OH were employed. the results revealed that the measurements from the different assays were not in agreement, indicating that the methods should not be used interchangeably for measurement of equine ACE activity. Rather, a single method of analysis should be adopted to achieve comparable results and critical appraisal of the literature is needed when attempting to compare results obtained from different assays.en
dc.description.affiliationUniv Melbourne, Fac Vet Sci, Melbourne, Vic 3010, Australia
dc.description.affiliationUniv Melbourne, BIO Inst 21, Melbourne, Vic 3010, Australia
dc.description.affiliationUniversidade Federal de São Paulo, BR-04023900 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, BR-04023900 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipUniversity of Melbourne (Australia)
dc.description.sponsorshipUNIFESP (Brazil)
dc.format.extent21-25
dc.identifierhttp://dx.doi.org/10.4142/jvs.2011.12.1.21
dc.identifier.citationJournal of Veterinary Science. Seoul: Korean Soc Veterinary Science, v. 12, n. 1, p. 21-25, 2011.
dc.identifier.doi10.4142/jvs.2011.12.1.21
dc.identifier.fileWOS000288473400004.pdf
dc.identifier.issn1229-845X
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/33497
dc.identifier.wosWOS:000288473400004
dc.language.isoeng
dc.publisherKorean Soc Veterinary Science
dc.relation.ispartofJournal of Veterinary Science
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectangiotensia I-converting enzymeen
dc.subjectassay agreementen
dc.subjectbiochemistryen
dc.subjectequineen
dc.subjectmethodologyen
dc.titleDetermination of angiotensin I-converting enzyme activity in equine blood: lack of agreement between methods of analysisen
dc.typeinfo:eu-repo/semantics/article
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