Action of plant proteinase inhibitors on enzymes of physiopathological importance

Detalhes bibliográficos
Autor(a) principal: Oliva,Maria Luiza V.
Data de Publicação: 2009
Outros Autores: Sampaio,Misako U.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Anais da Academia Brasileira de Ciências (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652009000300023
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.
id ABC-1_acb262f3c8acc9f7d81bfdeca2e21fa4
oai_identifier_str oai:scielo:S0001-37652009000300023
network_acronym_str ABC-1
network_name_str Anais da Academia Brasileira de Ciências (Online)
repository_id_str
spelling 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.Academia Brasileira de Ciências2009-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652009000300023Anais da Academia Brasileira de Ciências v.81 n.3 2009reponame:Anais da Academia Brasileira de Ciências (Online)instname:Academia Brasileira de Ciências (ABC)instacron:ABC10.1590/S0001-37652009000300023info:eu-repo/semantics/openAccessOliva,Maria Luiza V.Sampaio,Misako U.eng2009-08-20T00:00:00Zoai:scielo:S0001-37652009000300023Revistahttp://www.scielo.br/aabchttps://old.scielo.br/oai/scielo-oai.php||aabc@abc.org.br1678-26900001-3765opendoar:2009-08-20T00:00Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC)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 V.
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 V.
author_facet Oliva,Maria Luiza V.
Sampaio,Misako U.
author_role author
author2 Sampaio,Misako U.
author2_role author
dc.contributor.author.fl_str_mv Oliva,Maria Luiza V.
Sampaio,Misako U.
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
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=S0001-37652009000300023
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652009000300023
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0001-37652009000300023
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 Academia Brasileira de Ciências
publisher.none.fl_str_mv Academia Brasileira de Ciências
dc.source.none.fl_str_mv Anais da Academia Brasileira de Ciências v.81 n.3 2009
reponame:Anais da Academia Brasileira de Ciências (Online)
instname:Academia Brasileira de Ciências (ABC)
instacron:ABC
instname_str Academia Brasileira de Ciências (ABC)
instacron_str ABC
institution ABC
reponame_str Anais da Academia Brasileira de Ciências (Online)
collection Anais da Academia Brasileira de Ciências (Online)
repository.name.fl_str_mv Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC)
repository.mail.fl_str_mv ||aabc@abc.org.br
_version_ 1754302857303031808

Registros relacionados