Enzymatic activities and protein profile of latex from Calotropis procera

Detalhes bibliográficos
Autor(a) principal: Freitas, Cleverson Diniz T.
Data de Publicação: 2007
Outros Autores: Oliveira, Jefferson Soares, Miranda, Maria Raquel A., Macedo, Nívea Maria R., Sales, Maurício Pereira, Villas Boas, Laurival A., Ramos, Márcio Viana
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UFBA
Texto Completo: http://repositorio.ufba.br/ri/handle/ri/14450
Resumo: Texto completo: acesso restrito. p. 781-789
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spelling Freitas, Cleverson Diniz T.Oliveira, Jefferson SoaresMiranda, Maria Raquel A.Macedo, Nívea Maria R.Sales, Maurício PereiraVillas Boas, Laurival A.Ramos, Márcio VianaFreitas, Cleverson Diniz T.Oliveira, Jefferson SoaresMiranda, Maria Raquel A.Macedo, Nívea Maria R.Sales, Maurício PereiraVillas Boas, Laurival A.Ramos, Márcio Viana2014-01-23T16:52:59Z20070981-9428http://repositorio.ufba.br/ri/handle/ri/14450v. 45, n. 10-11Texto completo: acesso restrito. p. 781-789The laticifer fluid of Calotropis procera is rich in proteins and there is evidence that they are involved in the pharmacological properties of the latex. However, not much is known about how the latex-containing proteins are produced or their functions. In this study, laticifer proteins of C. procera were pooled and examined by 1D and 2D electrophoresis, masses spectrometry (MALDI-TOF) and characterized in respect of proteolytic activity and oxidative enzymes. Soluble laticifer proteins were predominantly composed of basic proteins (PI > 6.0) with molecular masses varying between 5 and 95 kDa. Proteins with a molecular mass of approximately 26,000 Da were more evident. Strong anti-oxidative activity of superoxide dismutase (EC 1.15.1.1) (1007.74 ± 91.89 U g−1 DM) and, to a lesser extent ascorbate peroxidase (EC 1.11.1.1) (0.117d ± 0.013 μMol H2O2 g−1 min−1), were detected. However, catalase (EC 1.11.1.6) was absent. The strong proteolytic activities of laticifer proteins from C. procera were shown to be shared by at least four distinct cysteine proteinases (EC 3.4.22.16) that were isolated by gel filtration chromatography. Serine and metaloproteinases were not detected and aspartic proteinase activities were barely visible. Chitinases (EC 3.2.1.14) were also isolated in a chitin column and their activities quantified. The presence of these enzymatic activities in latex from C. procera may confirm their involvement in resistance to phytopathogens and insects, mainly in its leaves where the latex circulates abundantly.Submitted by Suelen Reis (suziy.ellen@gmail.com) on 2014-01-14T15:25:49Z No. of bitstreams: 1 1-s2.0-S0981942807001611-main.pdf: 891719 bytes, checksum: bbe6914b49384aecafa43c84573a0cef (MD5)Approved for entry into archive by Alda Lima da Silva (sivalda@ufba.br) on 2014-01-23T16:52:59Z (GMT) No. of bitstreams: 1 1-s2.0-S0981942807001611-main.pdf: 891719 bytes, checksum: bbe6914b49384aecafa43c84573a0cef (MD5)Made available in DSpace on 2014-01-23T16:52:59Z (GMT). No. of bitstreams: 1 1-s2.0-S0981942807001611-main.pdf: 891719 bytes, checksum: bbe6914b49384aecafa43c84573a0cef (MD5) Previous issue date: 2007http://dx.doi.org/10.1016/j.plaphy.2007.07.020reponame:Repositório Institucional da UFBAinstname:Universidade Federal da Bahia (UFBA)instacron:UFBALatexProteolytic activityOxidative enzymesPlant defenseEnzymatic activities and protein profile of latex from Calotropis proceraPlant Physiology and Biochemistryinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article10000-01-01info:eu-repo/semantics/openAccessengORIGINAL1-s2.0-S0981942807001611-main.pdf1-s2.0-S0981942807001611-main.pdfapplication/pdf891719https://repositorio.ufba.br/bitstream/ri/14450/1/1-s2.0-S0981942807001611-main.pdfbbe6914b49384aecafa43c84573a0cefMD51LICENSElicense.txtlicense.txttext/plain1345https://repositorio.ufba.br/bitstream/ri/14450/2/license.txtff6eaa8b858ea317fded99f125f5fcd0MD52TEXT1-s2.0-S0981942807001611-main.pdf.txt1-s2.0-S0981942807001611-main.pdf.txtExtracted texttext/plain40497https://repositorio.ufba.br/bitstream/ri/14450/3/1-s2.0-S0981942807001611-main.pdf.txt4c5d5ce0062f3c461ba5a75c45480a95MD53ri/144502022-07-05 14:02:54.858oai:repositorio.ufba.br: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Repositório InstitucionalPUBhttp://192.188.11.11:8080/oai/requestopendoar:19322022-07-05T17:02:54Repositório Institucional da UFBA - Universidade Federal da Bahia (UFBA)false
dc.title.pt_BR.fl_str_mv Enzymatic activities and protein profile of latex from Calotropis procera
dc.title.alternative.pt_BR.fl_str_mv Plant Physiology and Biochemistry
title Enzymatic activities and protein profile of latex from Calotropis procera
spellingShingle Enzymatic activities and protein profile of latex from Calotropis procera
Freitas, Cleverson Diniz T.
Latex
Proteolytic activity
Oxidative enzymes
Plant defense
title_short Enzymatic activities and protein profile of latex from Calotropis procera
title_full Enzymatic activities and protein profile of latex from Calotropis procera
title_fullStr Enzymatic activities and protein profile of latex from Calotropis procera
title_full_unstemmed Enzymatic activities and protein profile of latex from Calotropis procera
title_sort Enzymatic activities and protein profile of latex from Calotropis procera
author Freitas, Cleverson Diniz T.
author_facet Freitas, Cleverson Diniz T.
Oliveira, Jefferson Soares
Miranda, Maria Raquel A.
Macedo, Nívea Maria R.
Sales, Maurício Pereira
Villas Boas, Laurival A.
Ramos, Márcio Viana
author_role author
author2 Oliveira, Jefferson Soares
Miranda, Maria Raquel A.
Macedo, Nívea Maria R.
Sales, Maurício Pereira
Villas Boas, Laurival A.
Ramos, Márcio Viana
author2_role author
author
author
author
author
author
dc.contributor.author.fl_str_mv Freitas, Cleverson Diniz T.
Oliveira, Jefferson Soares
Miranda, Maria Raquel A.
Macedo, Nívea Maria R.
Sales, Maurício Pereira
Villas Boas, Laurival A.
Ramos, Márcio Viana
Freitas, Cleverson Diniz T.
Oliveira, Jefferson Soares
Miranda, Maria Raquel A.
Macedo, Nívea Maria R.
Sales, Maurício Pereira
Villas Boas, Laurival A.
Ramos, Márcio Viana
dc.subject.por.fl_str_mv Latex
Proteolytic activity
Oxidative enzymes
Plant defense
topic Latex
Proteolytic activity
Oxidative enzymes
Plant defense
description Texto completo: acesso restrito. p. 781-789
publishDate 2007
dc.date.issued.fl_str_mv 2007
dc.date.accessioned.fl_str_mv 2014-01-23T16:52:59Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://repositorio.ufba.br/ri/handle/ri/14450
dc.identifier.issn.none.fl_str_mv 0981-9428
dc.identifier.number.pt_BR.fl_str_mv v. 45, n. 10-11
identifier_str_mv 0981-9428
v. 45, n. 10-11
url http://repositorio.ufba.br/ri/handle/ri/14450
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.pt_BR.fl_str_mv http://dx.doi.org/10.1016/j.plaphy.2007.07.020
dc.source.none.fl_str_mv reponame:Repositório Institucional da UFBA
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reponame_str Repositório Institucional da UFBA
collection Repositório Institucional da UFBA
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