Purification and Characterization of Four New Cysteine Endopeptidases From Fruits of <i>Bromelia pinguin</i> L. Grown in Cuba
- Autores
- Abreu Payrol, Juan; Obregón, Walter David; Trejo, Sebastián Alejandro; Caffini, Néstor Oscar
- Año de publicación
- 2008
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Bromelia pinguin L. is a plant broadly distributed in Central America and Caribbean islands. The fruits have been used in traditional medicine as anthelmintic, probably owed to the presence of a mixture of cysteine endopeptidases, initially termed pinguinain. This work deals with the purification and characterization of the four main components of that mixture, two of them showing acid pI and the other two alkaline pI. Molecular masses (SDS-PAGE and MALDI-TOF), N-terminal sequence and the reactivity and kinetic parameters versus synthetic substrates (p-nitrophenyl-N-α-CBZ-amino acid esters, PFLNA, Z-Arg-Arg-p-NA, and Z-Phe-Arg-p-NA) of the studied peptidases are given, as well as the N-terminal sequences of the enzymes and the homology degree with other plant endopeptidases.
Facultad de Ciencias Exactas
Centro de Investigación de Proteínas Vegetales - Materia
-
Ciencias Exactas
Biología
Bromelia pinguin L.
Bromeliaceae
Plant cysteine endopeptidases
Pinguinain - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by/4.0/
- Repositorio
.jpg)
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/133375
Ver los metadatos del registro completo
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Purification and Characterization of Four New Cysteine Endopeptidases From Fruits of <i>Bromelia pinguin</i> L. Grown in CubaAbreu Payrol, JuanObregón, Walter DavidTrejo, Sebastián AlejandroCaffini, Néstor OscarCiencias ExactasBiologíaBromelia pinguin L.BromeliaceaePlant cysteine endopeptidasesPinguinain<i>Bromelia pinguin</i> L. is a plant broadly distributed in Central America and Caribbean islands. The fruits have been used in traditional medicine as anthelmintic, probably owed to the presence of a mixture of cysteine endopeptidases, initially termed pinguinain. This work deals with the purification and characterization of the four main components of that mixture, two of them showing acid pI and the other two alkaline pI. Molecular masses (SDS-PAGE and MALDI-TOF), N-terminal sequence and the reactivity and kinetic parameters versus synthetic substrates (p-nitrophenyl-N-α-CBZ-amino acid esters, PFLNA, Z-Arg-Arg-p-NA, and Z-Phe-Arg-p-NA) of the studied peptidases are given, as well as the N-terminal sequences of the enzymes and the homology degree with other plant endopeptidases.Facultad de Ciencias ExactasCentro de Investigación de Proteínas Vegetales2008-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf88-96http://sedici.unlp.edu.ar/handle/10915/133375enginfo:eu-repo/semantics/altIdentifier/issn/1572-3887info:eu-repo/semantics/altIdentifier/issn/1573-4943info:eu-repo/semantics/altIdentifier/issn/0277-8033info:eu-repo/semantics/altIdentifier/doi/10.1007/s10930-007-9111-2info:eu-repo/semantics/altIdentifier/pmid/17932734info: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:UNLP2025-09-29T11:31:52Zoai:sedici.unlp.edu.ar:10915/133375Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:31:52.514SEDICI (UNLP) - Universidad Nacional de La Platafalse |
| dc.title.none.fl_str_mv |
Purification and Characterization of Four New Cysteine Endopeptidases From Fruits of <i>Bromelia pinguin</i> L. Grown in Cuba |
| title |
Purification and Characterization of Four New Cysteine Endopeptidases From Fruits of <i>Bromelia pinguin</i> L. Grown in Cuba |
| spellingShingle |
Purification and Characterization of Four New Cysteine Endopeptidases From Fruits of <i>Bromelia pinguin</i> L. Grown in Cuba Abreu Payrol, Juan Ciencias Exactas Biología Bromelia pinguin L. Bromeliaceae Plant cysteine endopeptidases Pinguinain |
| title_short |
Purification and Characterization of Four New Cysteine Endopeptidases From Fruits of <i>Bromelia pinguin</i> L. Grown in Cuba |
| title_full |
Purification and Characterization of Four New Cysteine Endopeptidases From Fruits of <i>Bromelia pinguin</i> L. Grown in Cuba |
| title_fullStr |
Purification and Characterization of Four New Cysteine Endopeptidases From Fruits of <i>Bromelia pinguin</i> L. Grown in Cuba |
| title_full_unstemmed |
Purification and Characterization of Four New Cysteine Endopeptidases From Fruits of <i>Bromelia pinguin</i> L. Grown in Cuba |
| title_sort |
Purification and Characterization of Four New Cysteine Endopeptidases From Fruits of <i>Bromelia pinguin</i> L. Grown in Cuba |
| dc.creator.none.fl_str_mv |
Abreu Payrol, Juan Obregón, Walter David Trejo, Sebastián Alejandro Caffini, Néstor Oscar |
| author |
Abreu Payrol, Juan |
| author_facet |
Abreu Payrol, Juan Obregón, Walter David Trejo, Sebastián Alejandro Caffini, Néstor Oscar |
| author_role |
author |
| author2 |
Obregón, Walter David Trejo, Sebastián Alejandro Caffini, Néstor Oscar |
| author2_role |
author author author |
| dc.subject.none.fl_str_mv |
Ciencias Exactas Biología Bromelia pinguin L. Bromeliaceae Plant cysteine endopeptidases Pinguinain |
| topic |
Ciencias Exactas Biología Bromelia pinguin L. Bromeliaceae Plant cysteine endopeptidases Pinguinain |
| dc.description.none.fl_txt_mv |
<i>Bromelia pinguin</i> L. is a plant broadly distributed in Central America and Caribbean islands. The fruits have been used in traditional medicine as anthelmintic, probably owed to the presence of a mixture of cysteine endopeptidases, initially termed pinguinain. This work deals with the purification and characterization of the four main components of that mixture, two of them showing acid pI and the other two alkaline pI. Molecular masses (SDS-PAGE and MALDI-TOF), N-terminal sequence and the reactivity and kinetic parameters versus synthetic substrates (p-nitrophenyl-N-α-CBZ-amino acid esters, PFLNA, Z-Arg-Arg-p-NA, and Z-Phe-Arg-p-NA) of the studied peptidases are given, as well as the N-terminal sequences of the enzymes and the homology degree with other plant endopeptidases. Facultad de Ciencias Exactas Centro de Investigación de Proteínas Vegetales |
| description |
<i>Bromelia pinguin</i> L. is a plant broadly distributed in Central America and Caribbean islands. The fruits have been used in traditional medicine as anthelmintic, probably owed to the presence of a mixture of cysteine endopeptidases, initially termed pinguinain. This work deals with the purification and characterization of the four main components of that mixture, two of them showing acid pI and the other two alkaline pI. Molecular masses (SDS-PAGE and MALDI-TOF), N-terminal sequence and the reactivity and kinetic parameters versus synthetic substrates (p-nitrophenyl-N-α-CBZ-amino acid esters, PFLNA, Z-Arg-Arg-p-NA, and Z-Phe-Arg-p-NA) of the studied peptidases are given, as well as the N-terminal sequences of the enzymes and the homology degree with other plant endopeptidases. |
| publishDate |
2008 |
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2008-02 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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http://sedici.unlp.edu.ar/handle/10915/133375 |
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eng |
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eng |
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