Isolation and partial purification of beta-galactosidases from cotyledons of two cowpea cultivars
Autor(a) principal: | |
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Data de Publicação: | 2001 |
Outros Autores: | , , , |
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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Revista Brasileira de Fisiologia Vegetal (Online) |
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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 |
_version_ |
1754820904282488832 |