Isolation and partial purification of beta-galactosidases from cotyledons of two cowpea cultivars

Detalhes bibliográficos
Autor(a) principal: ENÉAS-FILHO,JOAQUIM
Data de Publicação: 2001
Outros Autores: BARBOSA,GISLAINY KARLA DA COSTA, SUDÉRIO,FABRÍCIO BONFIM, PRISCO,JOSÉ TARQUÍNIO, GOMES-FILHO,ENÉAS
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Revista Brasileira de Fisiologia Vegetal (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-31312001000300001
Resumo: Three isoforms of beta-galactosidases were isolated and partially purified from the cotyledons of quiescent seeds of Vita 3 and Vita 5 cowpea [Vigna unguiculata (L.) Walp.] cultivars differing in water and salt stress tolerance. The purification procedure consisted of ammonium sulfate fractionation, acid precipitation, ion exchange chromatography through DEAE-sephadex and affinity chromatography through Lactosyl-sepharose columns. The three isoforms isolated from the two cultivars showed the same chromatographic patterns, same optimum of temperature for enzyme activity assay (60ºC), identical thermal stability up to 50°C, and similar pH optima (3-4). However, they differed from each other in sensitivity towards metal ions and certain chemical agents presents in the assay medium. The results have shown that the observed differences in beta-galactosidases from the cotyledons of quiescent seeds were not sufficient to relate them to stress tolerance.
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spelling Isolation and partial purification of beta-galactosidases from cotyledons of two cowpea cultivarscotyledonsisozymesVigna unguiculataVita 3 and Vita 5 cultivarssalt toleranceThree isoforms of beta-galactosidases were isolated and partially purified from the cotyledons of quiescent seeds of Vita 3 and Vita 5 cowpea [Vigna unguiculata (L.) Walp.] cultivars differing in water and salt stress tolerance. The purification procedure consisted of ammonium sulfate fractionation, acid precipitation, ion exchange chromatography through DEAE-sephadex and affinity chromatography through Lactosyl-sepharose columns. The three isoforms isolated from the two cultivars showed the same chromatographic patterns, same optimum of temperature for enzyme activity assay (60ºC), identical thermal stability up to 50°C, and similar pH optima (3-4). However, they differed from each other in sensitivity towards metal ions and certain chemical agents presents in the assay medium. The results have shown that the observed differences in beta-galactosidases from the cotyledons of quiescent seeds were not sufficient to relate them to stress tolerance.Sociedade Brasileira de Fisiologia Vegetal2001-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-31312001000300001Revista Brasileira de Fisiologia Vegetal v.13 n.3 2001reponame:Revista Brasileira de Fisiologia Vegetal (Online)instname:Sociedade Brasileira de Fisiologia Vegetal (SBFV)instacron:SBFV10.1590/S0103-31312001000300001info:eu-repo/semantics/openAccessENÉAS-FILHO,JOAQUIMBARBOSA,GISLAINY KARLA DA COSTASUDÉRIO,FABRÍCIO BONFIMPRISCO,JOSÉ TARQUÍNIOGOMES-FILHO,ENÉASeng2002-07-16T00:00:00Zoai:scielo:S0103-31312001000300001Revistahttps://www.scielo.br/j/rbfv/ONGhttps://old.scielo.br/oai/scielo-oai.phppmazza@unicamp.br1806-93550103-3131opendoar:2002-07-16T00:00Revista Brasileira de Fisiologia Vegetal (Online) - Sociedade Brasileira de Fisiologia Vegetal (SBFV)false
dc.title.none.fl_str_mv Isolation and partial purification of beta-galactosidases from cotyledons of two cowpea cultivars
title Isolation and partial purification of beta-galactosidases from cotyledons of two cowpea cultivars
spellingShingle Isolation and partial purification of beta-galactosidases from cotyledons of two cowpea cultivars
ENÉAS-FILHO,JOAQUIM
cotyledons
isozymes
Vigna unguiculata
Vita 3 and Vita 5 cultivars
salt tolerance
title_short Isolation and partial purification of beta-galactosidases from cotyledons of two cowpea cultivars
title_full Isolation and partial purification of beta-galactosidases from cotyledons of two cowpea cultivars
title_fullStr Isolation and partial purification of beta-galactosidases from cotyledons of two cowpea cultivars
title_full_unstemmed Isolation and partial purification of beta-galactosidases from cotyledons of two cowpea cultivars
title_sort Isolation and partial purification of beta-galactosidases from cotyledons of two cowpea cultivars
author ENÉAS-FILHO,JOAQUIM
author_facet ENÉAS-FILHO,JOAQUIM
BARBOSA,GISLAINY KARLA DA COSTA
SUDÉRIO,FABRÍCIO BONFIM
PRISCO,JOSÉ TARQUÍNIO
GOMES-FILHO,ENÉAS
author_role author
author2 BARBOSA,GISLAINY KARLA DA COSTA
SUDÉRIO,FABRÍCIO BONFIM
PRISCO,JOSÉ TARQUÍNIO
GOMES-FILHO,ENÉAS
author2_role author
author
author
author
dc.contributor.author.fl_str_mv ENÉAS-FILHO,JOAQUIM
BARBOSA,GISLAINY KARLA DA COSTA
SUDÉRIO,FABRÍCIO BONFIM
PRISCO,JOSÉ TARQUÍNIO
GOMES-FILHO,ENÉAS
dc.subject.por.fl_str_mv cotyledons
isozymes
Vigna unguiculata
Vita 3 and Vita 5 cultivars
salt tolerance
topic cotyledons
isozymes
Vigna unguiculata
Vita 3 and Vita 5 cultivars
salt tolerance
description Three isoforms of beta-galactosidases were isolated and partially purified from the cotyledons of quiescent seeds of Vita 3 and Vita 5 cowpea [Vigna unguiculata (L.) Walp.] cultivars differing in water and salt stress tolerance. The purification procedure consisted of ammonium sulfate fractionation, acid precipitation, ion exchange chromatography through DEAE-sephadex and affinity chromatography through Lactosyl-sepharose columns. The three isoforms isolated from the two cultivars showed the same chromatographic patterns, same optimum of temperature for enzyme activity assay (60ºC), identical thermal stability up to 50°C, and similar pH optima (3-4). However, they differed from each other in sensitivity towards metal ions and certain chemical agents presents in the assay medium. The results have shown that the observed differences in beta-galactosidases from the cotyledons of quiescent seeds were not sufficient to relate them to stress tolerance.
publishDate 2001
dc.date.none.fl_str_mv 2001-01-01
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=S0103-31312001000300001
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-31312001000300001
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0103-31312001000300001
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 Fisiologia Vegetal
publisher.none.fl_str_mv Sociedade Brasileira de Fisiologia Vegetal
dc.source.none.fl_str_mv Revista Brasileira de Fisiologia Vegetal v.13 n.3 2001
reponame:Revista Brasileira de Fisiologia Vegetal (Online)
instname:Sociedade Brasileira de Fisiologia Vegetal (SBFV)
instacron:SBFV
instname_str Sociedade Brasileira de Fisiologia Vegetal (SBFV)
instacron_str SBFV
institution SBFV
reponame_str Revista Brasileira de Fisiologia Vegetal (Online)
collection Revista Brasileira de Fisiologia Vegetal (Online)
repository.name.fl_str_mv Revista Brasileira de Fisiologia Vegetal (Online) - Sociedade Brasileira de Fisiologia Vegetal (SBFV)
repository.mail.fl_str_mv pmazza@unicamp.br
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