Comparison of Two Cysteine Endopeptidases from Latices of Morrenia brachystephana Griseb. and Morrenia odorata (Hook et Arn.) Lindley (Asclepiadaceae)

Autores
Vairo Cavalli, Sandra Elizabeth; Cortadi, Adriana A.; Arribére, María Cecilia; Conforti, Paula Andrea; Caffini, Néstor Oscar; Priolo de Lufrano, Nora Silvia
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The properties of morrenain b II, a proteinase isolated from the latex of Morrenia brachystephana, were compared with those of morrenain o II, a proteinase obtained from the latex of Morrenia odorata. Both peptidases were purified to homogeneity by acetone precipitation followed by cation exchange chromatography. The enzymes have pi values higher than 9.3 and similar molecular masses (close to 26 kDa) as determined by SDS-PAGE. They display maximum proteolytic activity within an alkaline pH range, and also exhibit esterolytic activity. The N-terminal sequences of morrenain o II and morrenain b II show a high degree of homology between each other and to other cysteine plant proteinases.
Centro de Investigación de Proteínas Vegetales
Materia
Química
Biología
Latex peptidases
Morrenain
Protein purification
Thiol peptidases
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:10915/153185
Acceder
id SEDICI_ec02f664ff1a1a454ac1b0b251ef356f
oai_identifier_str oai:sedici.unlp.edu.ar:10915/153185
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Comparison of Two Cysteine Endopeptidases from Latices of Morrenia brachystephana Griseb. and Morrenia odorata (Hook et Arn.) Lindley (Asclepiadaceae)Vairo Cavalli, Sandra ElizabethCortadi, Adriana A.Arribére, María CeciliaConforti, Paula AndreaCaffini, Néstor OscarPriolo de Lufrano, Nora SilviaQuímicaBiologíaLatex peptidasesMorrenainProtein purificationThiol peptidasesThe properties of morrenain b II, a proteinase isolated from the latex of Morrenia brachystephana, were compared with those of morrenain o II, a proteinase obtained from the latex of Morrenia odorata. Both peptidases were purified to homogeneity by acetone precipitation followed by cation exchange chromatography. The enzymes have pi values higher than 9.3 and similar molecular masses (close to 26 kDa) as determined by SDS-PAGE. They display maximum proteolytic activity within an alkaline pH range, and also exhibit esterolytic activity. The N-terminal sequences of morrenain o II and morrenain b II show a high degree of homology between each other and to other cysteine plant proteinases.Centro de Investigación de Proteínas Vegetales2013info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/153185enginfo:eu-repo/semantics/altIdentifier/issn/1437-4315info:eu-repo/semantics/altIdentifier/doi/10.1515/bchm.2001.382.5.879/htmlinfo: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:UNLP2025-10-15T11:31:24Zoai:sedici.unlp.edu.ar:10915/153185Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-15 11:31:24.82SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Comparison of Two Cysteine Endopeptidases from Latices of Morrenia brachystephana Griseb. and Morrenia odorata (Hook et Arn.) Lindley (Asclepiadaceae)
title Comparison of Two Cysteine Endopeptidases from Latices of Morrenia brachystephana Griseb. and Morrenia odorata (Hook et Arn.) Lindley (Asclepiadaceae)
spellingShingle Comparison of Two Cysteine Endopeptidases from Latices of Morrenia brachystephana Griseb. and Morrenia odorata (Hook et Arn.) Lindley (Asclepiadaceae)
Vairo Cavalli, Sandra Elizabeth
Química
Biología
Latex peptidases
Morrenain
Protein purification
Thiol peptidases
title_short Comparison of Two Cysteine Endopeptidases from Latices of Morrenia brachystephana Griseb. and Morrenia odorata (Hook et Arn.) Lindley (Asclepiadaceae)
title_full Comparison of Two Cysteine Endopeptidases from Latices of Morrenia brachystephana Griseb. and Morrenia odorata (Hook et Arn.) Lindley (Asclepiadaceae)
title_fullStr Comparison of Two Cysteine Endopeptidases from Latices of Morrenia brachystephana Griseb. and Morrenia odorata (Hook et Arn.) Lindley (Asclepiadaceae)
title_full_unstemmed Comparison of Two Cysteine Endopeptidases from Latices of Morrenia brachystephana Griseb. and Morrenia odorata (Hook et Arn.) Lindley (Asclepiadaceae)
title_sort Comparison of Two Cysteine Endopeptidases from Latices of Morrenia brachystephana Griseb. and Morrenia odorata (Hook et Arn.) Lindley (Asclepiadaceae)
dc.creator.none.fl_str_mv Vairo Cavalli, Sandra Elizabeth
Cortadi, Adriana A.
Arribére, María Cecilia
Conforti, Paula Andrea
Caffini, Néstor Oscar
Priolo de Lufrano, Nora Silvia
author Vairo Cavalli, Sandra Elizabeth
author_facet Vairo Cavalli, Sandra Elizabeth
Cortadi, Adriana A.
Arribére, María Cecilia
Conforti, Paula Andrea
Caffini, Néstor Oscar
Priolo de Lufrano, Nora Silvia
author_role author
author2 Cortadi, Adriana A.
Arribére, María Cecilia
Conforti, Paula Andrea
Caffini, Néstor Oscar
Priolo de Lufrano, Nora Silvia
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Química
Biología
Latex peptidases
Morrenain
Protein purification
Thiol peptidases
topic Química
Biología
Latex peptidases
Morrenain
Protein purification
Thiol peptidases
dc.description.none.fl_txt_mv The properties of morrenain b II, a proteinase isolated from the latex of Morrenia brachystephana, were compared with those of morrenain o II, a proteinase obtained from the latex of Morrenia odorata. Both peptidases were purified to homogeneity by acetone precipitation followed by cation exchange chromatography. The enzymes have pi values higher than 9.3 and similar molecular masses (close to 26 kDa) as determined by SDS-PAGE. They display maximum proteolytic activity within an alkaline pH range, and also exhibit esterolytic activity. The N-terminal sequences of morrenain o II and morrenain b II show a high degree of homology between each other and to other cysteine plant proteinases.
Centro de Investigación de Proteínas Vegetales
description The properties of morrenain b II, a proteinase isolated from the latex of Morrenia brachystephana, were compared with those of morrenain o II, a proteinase obtained from the latex of Morrenia odorata. Both peptidases were purified to homogeneity by acetone precipitation followed by cation exchange chromatography. The enzymes have pi values higher than 9.3 and similar molecular masses (close to 26 kDa) as determined by SDS-PAGE. They display maximum proteolytic activity within an alkaline pH range, and also exhibit esterolytic activity. The N-terminal sequences of morrenain o II and morrenain b II show a high degree of homology between each other and to other cysteine plant proteinases.
publishDate 2013
dc.date.none.fl_str_mv 2013
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/10915/153185
url http://sedici.unlp.edu.ar/handle/10915/153185
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1437-4315
info:eu-repo/semantics/altIdentifier/doi/10.1515/bchm.2001.382.5.879/html
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
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
_version_ 1846064349977772032
score 13.221938

Publicaciones similares