Facile chemiluminescence assay for acyl-CoA oxidase activity: fundamentals and illustrative examples

Detalhes bibliográficos
Autor(a) principal: Yao,Min
Data de Publicação: 2014
Outros Autores: Xu,Xiangdong, Liu,Yang, Jiang,Lingling
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Journal of the Brazilian Chemical Society (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532014000400020
Resumo: Acyl-CoA oxidase (ACO) is the key enzyme that catalyzes the rate-determining step in the peroxisomal beta-oxidation of fatty acids. ACO catalyzes the oxidation of acyl-CoA with molecular oxygen to produce trans-2,3-dehydroacyl-CoA and H2O2. Given the participation of H2O2 in an enhanced chemiluminescent reaction with luminol, we have developed a novel "two-step" procedure for the quantitation of ACO activity by recording light emission using a chemiluminescence detector. A number of recommendations on standardizing the reaction conditions for the quantitative measurement of ACO-catalyzed reactions are offered. The proposed method is simple and reliable and has been successfully applied in the rat liver assay. The results indicate that ACO activities increased in the liver of type-2 diabetic rats but showed no significant change in the liver of insulin-resistant rat.
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spelling Facile chemiluminescence assay for acyl-CoA oxidase activity: fundamentals and illustrative examplesacyl-CoA oxidasechemiluminescenceluminolperoxisomal oxidationAcyl-CoA oxidase (ACO) is the key enzyme that catalyzes the rate-determining step in the peroxisomal beta-oxidation of fatty acids. ACO catalyzes the oxidation of acyl-CoA with molecular oxygen to produce trans-2,3-dehydroacyl-CoA and H2O2. Given the participation of H2O2 in an enhanced chemiluminescent reaction with luminol, we have developed a novel "two-step" procedure for the quantitation of ACO activity by recording light emission using a chemiluminescence detector. A number of recommendations on standardizing the reaction conditions for the quantitative measurement of ACO-catalyzed reactions are offered. The proposed method is simple and reliable and has been successfully applied in the rat liver assay. The results indicate that ACO activities increased in the liver of type-2 diabetic rats but showed no significant change in the liver of insulin-resistant rat.Sociedade Brasileira de Química2014-04-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532014000400020Journal of the Brazilian Chemical Society v.25 n.4 2014reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.5935/0103-5053.20140039info:eu-repo/semantics/openAccessYao,MinXu,XiangdongLiu,YangJiang,Linglingeng2014-04-22T00:00:00Zoai:scielo:S0103-50532014000400020Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2014-04-22T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false
dc.title.none.fl_str_mv Facile chemiluminescence assay for acyl-CoA oxidase activity: fundamentals and illustrative examples
title Facile chemiluminescence assay for acyl-CoA oxidase activity: fundamentals and illustrative examples
spellingShingle Facile chemiluminescence assay for acyl-CoA oxidase activity: fundamentals and illustrative examples
Yao,Min
acyl-CoA oxidase
chemiluminescence
luminol
peroxisomal oxidation
title_short Facile chemiluminescence assay for acyl-CoA oxidase activity: fundamentals and illustrative examples
title_full Facile chemiluminescence assay for acyl-CoA oxidase activity: fundamentals and illustrative examples
title_fullStr Facile chemiluminescence assay for acyl-CoA oxidase activity: fundamentals and illustrative examples
title_full_unstemmed Facile chemiluminescence assay for acyl-CoA oxidase activity: fundamentals and illustrative examples
title_sort Facile chemiluminescence assay for acyl-CoA oxidase activity: fundamentals and illustrative examples
author Yao,Min
author_facet Yao,Min
Xu,Xiangdong
Liu,Yang
Jiang,Lingling
author_role author
author2 Xu,Xiangdong
Liu,Yang
Jiang,Lingling
author2_role author
author
author
dc.contributor.author.fl_str_mv Yao,Min
Xu,Xiangdong
Liu,Yang
Jiang,Lingling
dc.subject.por.fl_str_mv acyl-CoA oxidase
chemiluminescence
luminol
peroxisomal oxidation
topic acyl-CoA oxidase
chemiluminescence
luminol
peroxisomal oxidation
description Acyl-CoA oxidase (ACO) is the key enzyme that catalyzes the rate-determining step in the peroxisomal beta-oxidation of fatty acids. ACO catalyzes the oxidation of acyl-CoA with molecular oxygen to produce trans-2,3-dehydroacyl-CoA and H2O2. Given the participation of H2O2 in an enhanced chemiluminescent reaction with luminol, we have developed a novel "two-step" procedure for the quantitation of ACO activity by recording light emission using a chemiluminescence detector. A number of recommendations on standardizing the reaction conditions for the quantitative measurement of ACO-catalyzed reactions are offered. The proposed method is simple and reliable and has been successfully applied in the rat liver assay. The results indicate that ACO activities increased in the liver of type-2 diabetic rats but showed no significant change in the liver of insulin-resistant rat.
publishDate 2014
dc.date.none.fl_str_mv 2014-04-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532014000400020
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532014000400020
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.5935/0103-5053.20140039
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Sociedade Brasileira de Química
publisher.none.fl_str_mv Sociedade Brasileira de Química
dc.source.none.fl_str_mv Journal of the Brazilian Chemical Society v.25 n.4 2014
reponame:Journal of the Brazilian Chemical Society (Online)
instname:Sociedade Brasileira de Química (SBQ)
instacron:SBQ
instname_str Sociedade Brasileira de Química (SBQ)
instacron_str SBQ
institution SBQ
reponame_str Journal of the Brazilian Chemical Society (Online)
collection Journal of the Brazilian Chemical Society (Online)
repository.name.fl_str_mv Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)
repository.mail.fl_str_mv ||office@jbcs.sbq.org.br
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