Morrenain b I, a Papain-like Endopeptidase from the Latex of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>)

Autores
Vairo Cavalli, Sandra Elizabeth; Arribére, María Cecilia; Cortadi, Adriana A.; Caffini, Néstor Oscar; Priolo de Lufrano, Nora Silvia
Año de publicación
2003
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A new cysteine endopeptidase (morrenain b I) has been purified and characterized from the latex of stems and petiols of Morrenia brachystephana Griseb. (Asclepiadaceae). Morrenain b I was the minor proteolytic component in the latex but showed higher specific activity than morrenain b II, which was the main active fraction. Both enzymes showed similar pH profiles and molecular masses, but kinetic parameters and N-terminal sequences were quite distinct, demonstrating that they are different enzymes instead of different forms of the same enzyme.
Centro de Investigación de Proteínas Vegetales
Materia
Biología
Química
Morrenia brachystephana
cysteine proteinase
morrenain b I
plant endopeptidase
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/139496
Acceder
id SEDICI_68457076cc5a4812014bc423c44a3c74
oai_identifier_str oai:sedici.unlp.edu.ar:10915/139496
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Morrenain b I, a Papain-like Endopeptidase from the Latex of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>)Vairo Cavalli, Sandra ElizabethArribére, María CeciliaCortadi, Adriana A.Caffini, Néstor OscarPriolo de Lufrano, Nora SilviaBiologíaQuímicaMorrenia brachystephanacysteine proteinasemorrenain b Iplant endopeptidaseA new cysteine endopeptidase (morrenain b I) has been purified and characterized from the latex of stems and petiols of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>). Morrenain b I was the minor proteolytic component in the latex but showed higher specific activity than morrenain b II, which was the main active fraction. Both enzymes showed similar pH profiles and molecular masses, but kinetic parameters and N-terminal sequences were quite distinct, demonstrating that they are different enzymes instead of different forms of the same enzyme.Centro de Investigación de Proteínas Vegetales2003-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf15-22http://sedici.unlp.edu.ar/handle/10915/139496enginfo:eu-repo/semantics/altIdentifier/issn/0277-8033info:eu-repo/semantics/altIdentifier/issn/1573-4943info:eu-repo/semantics/altIdentifier/doi/10.1023/a:1023059525861info:eu-repo/semantics/altIdentifier/pmid/12739894info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-11-05T13:11:26Zoai:sedici.unlp.edu.ar:10915/139496Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-11-05 13:11:26.316SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Morrenain b I, a Papain-like Endopeptidase from the Latex of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>)
title Morrenain b I, a Papain-like Endopeptidase from the Latex of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>)
spellingShingle Morrenain b I, a Papain-like Endopeptidase from the Latex of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>)
Vairo Cavalli, Sandra Elizabeth
Biología
Química
Morrenia brachystephana
cysteine proteinase
morrenain b I
plant endopeptidase
title_short Morrenain b I, a Papain-like Endopeptidase from the Latex of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>)
title_full Morrenain b I, a Papain-like Endopeptidase from the Latex of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>)
title_fullStr Morrenain b I, a Papain-like Endopeptidase from the Latex of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>)
title_full_unstemmed Morrenain b I, a Papain-like Endopeptidase from the Latex of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>)
title_sort Morrenain b I, a Papain-like Endopeptidase from the Latex of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>)
dc.creator.none.fl_str_mv Vairo Cavalli, Sandra Elizabeth
Arribére, María Cecilia
Cortadi, Adriana A.
Caffini, Néstor Oscar
Priolo de Lufrano, Nora Silvia
author Vairo Cavalli, Sandra Elizabeth
author_facet Vairo Cavalli, Sandra Elizabeth
Arribére, María Cecilia
Cortadi, Adriana A.
Caffini, Néstor Oscar
Priolo de Lufrano, Nora Silvia
author_role author
author2 Arribére, María Cecilia
Cortadi, Adriana A.
Caffini, Néstor Oscar
Priolo de Lufrano, Nora Silvia
author2_role author
author
author
author
dc.subject.none.fl_str_mv Biología
Química
Morrenia brachystephana
cysteine proteinase
morrenain b I
plant endopeptidase
topic Biología
Química
Morrenia brachystephana
cysteine proteinase
morrenain b I
plant endopeptidase
dc.description.none.fl_txt_mv A new cysteine endopeptidase (morrenain b I) has been purified and characterized from the latex of stems and petiols of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>). Morrenain b I was the minor proteolytic component in the latex but showed higher specific activity than morrenain b II, which was the main active fraction. Both enzymes showed similar pH profiles and molecular masses, but kinetic parameters and N-terminal sequences were quite distinct, demonstrating that they are different enzymes instead of different forms of the same enzyme.
Centro de Investigación de Proteínas Vegetales
description A new cysteine endopeptidase (morrenain b I) has been purified and characterized from the latex of stems and petiols of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>). Morrenain b I was the minor proteolytic component in the latex but showed higher specific activity than morrenain b II, which was the main active fraction. Both enzymes showed similar pH profiles and molecular masses, but kinetic parameters and N-terminal sequences were quite distinct, demonstrating that they are different enzymes instead of different forms of the same enzyme.
publishDate 2003
dc.date.none.fl_str_mv 2003-01
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/10915/139496
url http://sedici.unlp.edu.ar/handle/10915/139496
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0277-8033
info:eu-repo/semantics/altIdentifier/issn/1573-4943
info:eu-repo/semantics/altIdentifier/doi/10.1023/a:1023059525861
info:eu-repo/semantics/altIdentifier/pmid/12739894
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
15-22
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_ 1847978760103526400
score 13.082534

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