Facile chemiluminescence assay for acyl-CoA oxidase activity: fundamentals and illustrative examples
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , , |
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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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 |
_version_ |
1750318175800524800 |