Presence of multiple acid phosphatases activity in seedlings of cucumber, radish and rocket salad

Detalhes bibliográficos
Autor(a) principal: Tabaldi,Luciane Almeri
Data de Publicação: 2008
Outros Autores: Ruppenthal,Raquel, Pereira,Luciane Belmonte, Cargnelutti,Denise, Gonçalves,Jamile Fabbrin, Morsch,Vera Maria, Schetinger,Maria Rosa Chitolina
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Ciência Rural
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-84782008000300009
Resumo: Acid phosphatases (3.1.3.2) are a group of enzymes widely distributed in nature, which catalyze the hydrolysis of a variety of phosphate esters in the pH range of 4-6. We confirmed the presence of acid phosphatases in seedlings of cucumber (Cucumis sativus), radish (Raphanus sativus) and rocket salad (Eruca vesicaria) under different assay conditions using a rapid and simple preparation. The results showed that the optimum pH and temperature used for all species were close to 5.5 and 35°C, respectively. The enzyme was inhibited by molybdate, fluoride, azide, levamisole, orthovanadate, Zn2+ and Cu2+. Suramin had no effect on enzyme activity. The acid phosphatase from cucumber, radish and rocket salad hydrolyzed a wide variety of phosphate esters and the highest activity was observed with PPi, ATP and GTP. These results demonstrate that the enzyme investigated in this study is different from well known ester phosphate cleaving plant enzymes (apyrase and inorganic pyrophosphatases) and this preparation could be a useful tool to future toxicological studies and to study initially all isoforms of acid phosphatase.
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spelling Presence of multiple acid phosphatases activity in seedlings of cucumber, radish and rocket saladCucumis sativusRaphanus sativusEruca vesicariaphosphatasesAcid phosphatases (3.1.3.2) are a group of enzymes widely distributed in nature, which catalyze the hydrolysis of a variety of phosphate esters in the pH range of 4-6. We confirmed the presence of acid phosphatases in seedlings of cucumber (Cucumis sativus), radish (Raphanus sativus) and rocket salad (Eruca vesicaria) under different assay conditions using a rapid and simple preparation. The results showed that the optimum pH and temperature used for all species were close to 5.5 and 35°C, respectively. The enzyme was inhibited by molybdate, fluoride, azide, levamisole, orthovanadate, Zn2+ and Cu2+. Suramin had no effect on enzyme activity. The acid phosphatase from cucumber, radish and rocket salad hydrolyzed a wide variety of phosphate esters and the highest activity was observed with PPi, ATP and GTP. These results demonstrate that the enzyme investigated in this study is different from well known ester phosphate cleaving plant enzymes (apyrase and inorganic pyrophosphatases) and this preparation could be a useful tool to future toxicological studies and to study initially all isoforms of acid phosphatase.Universidade Federal de Santa Maria2008-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-84782008000300009Ciência Rural v.38 n.3 2008reponame:Ciência Ruralinstname:Universidade Federal de Santa Maria (UFSM)instacron:UFSM10.1590/S0103-84782008000300009info:eu-repo/semantics/openAccessTabaldi,Luciane AlmeriRuppenthal,RaquelPereira,Luciane BelmonteCargnelutti,DeniseGonçalves,Jamile FabbrinMorsch,Vera MariaSchetinger,Maria Rosa Chitolinaeng2008-04-04T00:00:00ZRevista
dc.title.none.fl_str_mv Presence of multiple acid phosphatases activity in seedlings of cucumber, radish and rocket salad
title Presence of multiple acid phosphatases activity in seedlings of cucumber, radish and rocket salad
spellingShingle Presence of multiple acid phosphatases activity in seedlings of cucumber, radish and rocket salad
Tabaldi,Luciane Almeri
Cucumis sativus
Raphanus sativus
Eruca vesicaria
phosphatases
title_short Presence of multiple acid phosphatases activity in seedlings of cucumber, radish and rocket salad
title_full Presence of multiple acid phosphatases activity in seedlings of cucumber, radish and rocket salad
title_fullStr Presence of multiple acid phosphatases activity in seedlings of cucumber, radish and rocket salad
title_full_unstemmed Presence of multiple acid phosphatases activity in seedlings of cucumber, radish and rocket salad
title_sort Presence of multiple acid phosphatases activity in seedlings of cucumber, radish and rocket salad
author Tabaldi,Luciane Almeri
author_facet Tabaldi,Luciane Almeri
Ruppenthal,Raquel
Pereira,Luciane Belmonte
Cargnelutti,Denise
Gonçalves,Jamile Fabbrin
Morsch,Vera Maria
Schetinger,Maria Rosa Chitolina
author_role author
author2 Ruppenthal,Raquel
Pereira,Luciane Belmonte
Cargnelutti,Denise
Gonçalves,Jamile Fabbrin
Morsch,Vera Maria
Schetinger,Maria Rosa Chitolina
author2_role author
author
author
author
author
author
dc.contributor.author.fl_str_mv Tabaldi,Luciane Almeri
Ruppenthal,Raquel
Pereira,Luciane Belmonte
Cargnelutti,Denise
Gonçalves,Jamile Fabbrin
Morsch,Vera Maria
Schetinger,Maria Rosa Chitolina
dc.subject.por.fl_str_mv Cucumis sativus
Raphanus sativus
Eruca vesicaria
phosphatases
topic Cucumis sativus
Raphanus sativus
Eruca vesicaria
phosphatases
description Acid phosphatases (3.1.3.2) are a group of enzymes widely distributed in nature, which catalyze the hydrolysis of a variety of phosphate esters in the pH range of 4-6. We confirmed the presence of acid phosphatases in seedlings of cucumber (Cucumis sativus), radish (Raphanus sativus) and rocket salad (Eruca vesicaria) under different assay conditions using a rapid and simple preparation. The results showed that the optimum pH and temperature used for all species were close to 5.5 and 35°C, respectively. The enzyme was inhibited by molybdate, fluoride, azide, levamisole, orthovanadate, Zn2+ and Cu2+. Suramin had no effect on enzyme activity. The acid phosphatase from cucumber, radish and rocket salad hydrolyzed a wide variety of phosphate esters and the highest activity was observed with PPi, ATP and GTP. These results demonstrate that the enzyme investigated in this study is different from well known ester phosphate cleaving plant enzymes (apyrase and inorganic pyrophosphatases) and this preparation could be a useful tool to future toxicological studies and to study initially all isoforms of acid phosphatase.
publishDate 2008
dc.date.none.fl_str_mv 2008-06-01
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=S0103-84782008000300009
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-84782008000300009
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0103-84782008000300009
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 Universidade Federal de Santa Maria
publisher.none.fl_str_mv Universidade Federal de Santa Maria
dc.source.none.fl_str_mv Ciência Rural v.38 n.3 2008
reponame:Ciência Rural
instname:Universidade Federal de Santa Maria (UFSM)
instacron:UFSM
instname_str Universidade Federal de Santa Maria (UFSM)
instacron_str UFSM
institution UFSM
reponame_str Ciência Rural
collection Ciência Rural
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repository.mail.fl_str_mv
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