Action of plant proteinase inhibitors on enzymes of physiopathological importance
Autor(a) principal: | |
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Data de Publicação: | 2009 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://dx.doi.org/10.1590/S0001-37652009000300023 http://repositorio.unifesp.br/handle/11600/42527 |
Resumo: | Obtained from leguminous seeds, various plant proteins inhibit animal proteinases, including human, and can be considered for the development of compounds with biological activity. Inhibitors from the Bowman-Birk and plant Kunitz-type family have been characterized by proteinase specificity, primary structure and reactive site. Our group mostly studies the genus Bauhinia, mainly the species bauhinioides, rufa, ungulata and variegata. In some species, more than one inhibitor was characterized, exhibiting different properties. Although proteins from this group share high structural similarity, they present differences in proteinase inhibition, explored in studies using diverse biological models. |
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Repositório Institucional da UNIFESP |
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Action of plant proteinase inhibitors on enzymes of physiopathological importanceBowman-BirkchymotrypsinKunitz inhibitorsplasma kallikreinprimary structuretrypsinObtained from leguminous seeds, various plant proteins inhibit animal proteinases, including human, and can be considered for the development of compounds with biological activity. Inhibitors from the Bowman-Birk and plant Kunitz-type family have been characterized by proteinase specificity, primary structure and reactive site. Our group mostly studies the genus Bauhinia, mainly the species bauhinioides, rufa, ungulata and variegata. In some species, more than one inhibitor was characterized, exhibiting different properties. Although proteins from this group share high structural similarity, they present differences in proteinase inhibition, explored in studies using diverse biological models.Univ Fed Sao Paulo, Dept Bioquim, Escola Paulista Med, BR-04044020 Sao Paulo, BrazilUniv Fed Sao Paulo, Dept Bioquim, Escola Paulista Med, BR-04044020 Sao Paulo, BrazilWeb of ScienceCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Fundo de Auxilio aos Docentes e Alunos/Fundacao de Apoio a UNIFESP (FADA/FAP)Acad Brasileira De CienciasUniversidade Federal de São Paulo (UNIFESP)Oliva, Maria Luiza Vilela [UNIFESP]Sampaio, Misako Uemura [UNIFESP]2018-06-15T13:50:09Z2018-06-15T13:50:09Z2009-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion615-621http://dx.doi.org/10.1590/S0001-37652009000300023Anais Da Academia Brasileira De Ciencias. Rio Janeiro: Acad Brasileira De Ciencias, v. 81, n. 3, p. 615-621, 2009.10.1590/S0001-37652009000300023S0001-37652009000300023.pdf0001-3765S0001-37652009000300023http://repositorio.unifesp.br/handle/11600/42527WOS:000269462300023engAnais Da Academia Brasileira De Cienciasinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2024-05-02T11:58:37Zoai:repositorio.unifesp.br/:11600/42527Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-05-02T11:58:37Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.none.fl_str_mv |
Action of plant proteinase inhibitors on enzymes of physiopathological importance |
title |
Action of plant proteinase inhibitors on enzymes of physiopathological importance |
spellingShingle |
Action of plant proteinase inhibitors on enzymes of physiopathological importance Oliva, Maria Luiza Vilela [UNIFESP] Bowman-Birk chymotrypsin Kunitz inhibitors plasma kallikrein primary structure trypsin |
title_short |
Action of plant proteinase inhibitors on enzymes of physiopathological importance |
title_full |
Action of plant proteinase inhibitors on enzymes of physiopathological importance |
title_fullStr |
Action of plant proteinase inhibitors on enzymes of physiopathological importance |
title_full_unstemmed |
Action of plant proteinase inhibitors on enzymes of physiopathological importance |
title_sort |
Action of plant proteinase inhibitors on enzymes of physiopathological importance |
author |
Oliva, Maria Luiza Vilela [UNIFESP] |
author_facet |
Oliva, Maria Luiza Vilela [UNIFESP] Sampaio, Misako Uemura [UNIFESP] |
author_role |
author |
author2 |
Sampaio, Misako Uemura [UNIFESP] |
author2_role |
author |
dc.contributor.none.fl_str_mv |
Universidade Federal de São Paulo (UNIFESP) |
dc.contributor.author.fl_str_mv |
Oliva, Maria Luiza Vilela [UNIFESP] Sampaio, Misako Uemura [UNIFESP] |
dc.subject.por.fl_str_mv |
Bowman-Birk chymotrypsin Kunitz inhibitors plasma kallikrein primary structure trypsin |
topic |
Bowman-Birk chymotrypsin Kunitz inhibitors plasma kallikrein primary structure trypsin |
description |
Obtained from leguminous seeds, various plant proteins inhibit animal proteinases, including human, and can be considered for the development of compounds with biological activity. Inhibitors from the Bowman-Birk and plant Kunitz-type family have been characterized by proteinase specificity, primary structure and reactive site. Our group mostly studies the genus Bauhinia, mainly the species bauhinioides, rufa, ungulata and variegata. In some species, more than one inhibitor was characterized, exhibiting different properties. Although proteins from this group share high structural similarity, they present differences in proteinase inhibition, explored in studies using diverse biological models. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-09-01 2018-06-15T13:50:09Z 2018-06-15T13:50:09Z |
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://dx.doi.org/10.1590/S0001-37652009000300023 Anais Da Academia Brasileira De Ciencias. Rio Janeiro: Acad Brasileira De Ciencias, v. 81, n. 3, p. 615-621, 2009. 10.1590/S0001-37652009000300023 S0001-37652009000300023.pdf 0001-3765 S0001-37652009000300023 http://repositorio.unifesp.br/handle/11600/42527 WOS:000269462300023 |
url |
http://dx.doi.org/10.1590/S0001-37652009000300023 http://repositorio.unifesp.br/handle/11600/42527 |
identifier_str_mv |
Anais Da Academia Brasileira De Ciencias. Rio Janeiro: Acad Brasileira De Ciencias, v. 81, n. 3, p. 615-621, 2009. 10.1590/S0001-37652009000300023 S0001-37652009000300023.pdf 0001-3765 S0001-37652009000300023 WOS:000269462300023 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Anais Da Academia Brasileira De Ciencias |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
615-621 |
dc.publisher.none.fl_str_mv |
Acad Brasileira De Ciencias |
publisher.none.fl_str_mv |
Acad Brasileira De Ciencias |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
instname_str |
Universidade Federal de São Paulo (UNIFESP) |
instacron_str |
UNIFESP |
institution |
UNIFESP |
reponame_str |
Repositório Institucional da UNIFESP |
collection |
Repositório Institucional da UNIFESP |
repository.name.fl_str_mv |
Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
biblioteca.csp@unifesp.br |
_version_ |
1814268436563361792 |