Presence of multiple acid phosphatases activity in seedlings of cucumber, radish and rocket salad
Autor(a) principal: | |
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Data de Publicação: | 2008 |
Outros Autores: | , , , , , |
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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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 |
repository.name.fl_str_mv |
|
repository.mail.fl_str_mv |
|
_version_ |
1749140530184323072 |