Proteolytic properties of <i>Funastrum clausum</i> latex

Autores
Morcelle del Valle, Susana Raquel; Caffini, Néstor Oscar; Priolo de Lufrano, Nora Silvia
Año de publicación
2004
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
As part of a screening of latex endopeptidases from plants growing in Argentina, the presence of proteolytic activity in the latex of Funastrum clausum stems is reported. The proteases present in the crude extract showed the main characteristics of the cysteine proteolytic class, i.e. optimum pH at alkaline range, isoelectric point (pI) higher than 9.0, and inhibition of proteolytic activity by thiol blocking reagents. A remarkable thermal stability was also evident in the crude extract. Endosterolytic preference tried on p-nitrophenyl esters of N-a-carbobenzoxy-L-amino acids was higher for the alanine, asparagine and tyrosine derivatives. Preliminary peptidase purification by two-step ionic exchange showed the presence of two proteolytic fractions with molecular masses of approximately 24.0 kDa according to SDS-PAGE.
Centro de Investigación de Proteínas Vegetales
Materia
Biología
<i>Funastrum clausum</i>
Latex
Thiol proteases
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/97750
Acceder
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network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Proteolytic properties of <i>Funastrum clausum</i> latexMorcelle del Valle, Susana RaquelCaffini, Néstor OscarPriolo de Lufrano, Nora SilviaBiología<i>Funastrum clausum</i>LatexThiol proteasesAs part of a screening of latex endopeptidases from plants growing in Argentina, the presence of proteolytic activity in the latex of Funastrum clausum stems is reported. The proteases present in the crude extract showed the main characteristics of the cysteine proteolytic class, i.e. optimum pH at alkaline range, isoelectric point (pI) higher than 9.0, and inhibition of proteolytic activity by thiol blocking reagents. A remarkable thermal stability was also evident in the crude extract. Endosterolytic preference tried on p-nitrophenyl esters of N-a-carbobenzoxy-L-amino acids was higher for the alanine, asparagine and tyrosine derivatives. Preliminary peptidase purification by two-step ionic exchange showed the presence of two proteolytic fractions with molecular masses of approximately 24.0 kDa according to SDS-PAGE.Centro de Investigación de Proteínas Vegetales2004info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf480-493http://sedici.unlp.edu.ar/handle/10915/97750enginfo:eu-repo/semantics/altIdentifier/issn/0367-326Xinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.fitote.2004.04.006info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-10T12:23:51Zoai:sedici.unlp.edu.ar:10915/97750Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-10 12:23:51.528SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Proteolytic properties of <i>Funastrum clausum</i> latex
title Proteolytic properties of <i>Funastrum clausum</i> latex
spellingShingle Proteolytic properties of <i>Funastrum clausum</i> latex
Morcelle del Valle, Susana Raquel
Biología
<i>Funastrum clausum</i>
Latex
Thiol proteases
title_short Proteolytic properties of <i>Funastrum clausum</i> latex
title_full Proteolytic properties of <i>Funastrum clausum</i> latex
title_fullStr Proteolytic properties of <i>Funastrum clausum</i> latex
title_full_unstemmed Proteolytic properties of <i>Funastrum clausum</i> latex
title_sort Proteolytic properties of <i>Funastrum clausum</i> latex
dc.creator.none.fl_str_mv Morcelle del Valle, Susana Raquel
Caffini, Néstor Oscar
Priolo de Lufrano, Nora Silvia
author Morcelle del Valle, Susana Raquel
author_facet Morcelle del Valle, Susana Raquel
Caffini, Néstor Oscar
Priolo de Lufrano, Nora Silvia
author_role author
author2 Caffini, Néstor Oscar
Priolo de Lufrano, Nora Silvia
author2_role author
author
dc.subject.none.fl_str_mv Biología
<i>Funastrum clausum</i>
Latex
Thiol proteases
topic Biología
<i>Funastrum clausum</i>
Latex
Thiol proteases
dc.description.none.fl_txt_mv As part of a screening of latex endopeptidases from plants growing in Argentina, the presence of proteolytic activity in the latex of Funastrum clausum stems is reported. The proteases present in the crude extract showed the main characteristics of the cysteine proteolytic class, i.e. optimum pH at alkaline range, isoelectric point (pI) higher than 9.0, and inhibition of proteolytic activity by thiol blocking reagents. A remarkable thermal stability was also evident in the crude extract. Endosterolytic preference tried on p-nitrophenyl esters of N-a-carbobenzoxy-L-amino acids was higher for the alanine, asparagine and tyrosine derivatives. Preliminary peptidase purification by two-step ionic exchange showed the presence of two proteolytic fractions with molecular masses of approximately 24.0 kDa according to SDS-PAGE.
Centro de Investigación de Proteínas Vegetales
description As part of a screening of latex endopeptidases from plants growing in Argentina, the presence of proteolytic activity in the latex of Funastrum clausum stems is reported. The proteases present in the crude extract showed the main characteristics of the cysteine proteolytic class, i.e. optimum pH at alkaline range, isoelectric point (pI) higher than 9.0, and inhibition of proteolytic activity by thiol blocking reagents. A remarkable thermal stability was also evident in the crude extract. Endosterolytic preference tried on p-nitrophenyl esters of N-a-carbobenzoxy-L-amino acids was higher for the alanine, asparagine and tyrosine derivatives. Preliminary peptidase purification by two-step ionic exchange showed the presence of two proteolytic fractions with molecular masses of approximately 24.0 kDa according to SDS-PAGE.
publishDate 2004
dc.date.none.fl_str_mv 2004
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/97750
url http://sedici.unlp.edu.ar/handle/10915/97750
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0367-326X
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.fitote.2004.04.006
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
480-493
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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