Two new cysteine endopeptidases obtained from the latex of Araujia hortorum fruits

Autores
Obregón, Walter David; Arribére, María Cecilia; Morcelle del Valle, Susana Raquel; Liggieri, Constanza Silvina; Caffini, Néstor Oscar; Priolo de Lufrano, Nora Silvia
Año de publicación
2001
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Two new endopeptidases were purified to homogeneity from the latex of Araujia hortorum fruits by a simple purification procedure involving ultracentrifugation and ion exchange chromatography. Molecular weights of araujiain h II and araujiain h III were 23,718 and 23546 (mass spectrometry), respectively. The isoelectric point of araujiain h II was 8.9, whereas araujiain h III had a pI higher than 9.3. Maximum proteolytic activity on caseine was reached at pH 8.0-9.0 for both endopeptidases, which were irreversibly inhibited by iodoacetate and E-64, suggesting they belong to the cysteine protease family. Esterolytic activity was determined on N-alpha-CBZ-amino acid-p-nitrophenyl esters, and the highest kcat/Km values for the both enzymes were obtained with the glutamine derivative. The N-terminal sequences of araujiain h II and araujiain h III showed a high degree of homology with other plant cysteine endopeptidases.
Centro de Investigación de Proteínas Vegetales
Materia
Química
Araujiain
Cysteine endopeptidases
Latex
Milkweed family
Protein purification
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:10915/143564
Acceder
id SEDICI_9e074d20e73000be87fd7dd76e111374
oai_identifier_str oai:sedici.unlp.edu.ar:10915/143564
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Two new cysteine endopeptidases obtained from the latex of Araujia hortorum fruitsObregón, Walter DavidArribére, María CeciliaMorcelle del Valle, Susana RaquelLiggieri, Constanza SilvinaCaffini, Néstor OscarPriolo de Lufrano, Nora SilviaQuímicaAraujiainCysteine endopeptidasesLatexMilkweed familyProtein purificationTwo new endopeptidases were purified to homogeneity from the latex of Araujia hortorum fruits by a simple purification procedure involving ultracentrifugation and ion exchange chromatography. Molecular weights of araujiain h II and araujiain h III were 23,718 and 23546 (mass spectrometry), respectively. The isoelectric point of araujiain h II was 8.9, whereas araujiain h III had a pI higher than 9.3. Maximum proteolytic activity on caseine was reached at pH 8.0-9.0 for both endopeptidases, which were irreversibly inhibited by iodoacetate and E-64, suggesting they belong to the cysteine protease family. Esterolytic activity was determined on N-alpha-CBZ-amino acid-p-nitrophenyl esters, and the highest kcat/Km values for the both enzymes were obtained with the glutamine derivative. The N-terminal sequences of araujiain h II and araujiain h III showed a high degree of homology with other plant cysteine endopeptidases.Centro de Investigación de Proteínas Vegetales2001info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf317-325http://sedici.unlp.edu.ar/handle/10915/143564enginfo:eu-repo/semantics/altIdentifier/issn/0277-8033info:eu-repo/semantics/altIdentifier/issn/1573-4943info:eu-repo/semantics/altIdentifier/doi/10.1023/a:1010953718679info:eu-repo/semantics/altIdentifier/pmid/11594466info: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:UNLP2025-09-29T11:32:36Zoai:sedici.unlp.edu.ar:10915/143564Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:32:36.921SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Two new cysteine endopeptidases obtained from the latex of Araujia hortorum fruits
title Two new cysteine endopeptidases obtained from the latex of Araujia hortorum fruits
spellingShingle Two new cysteine endopeptidases obtained from the latex of Araujia hortorum fruits
Obregón, Walter David
Química
Araujiain
Cysteine endopeptidases
Latex
Milkweed family
Protein purification
title_short Two new cysteine endopeptidases obtained from the latex of Araujia hortorum fruits
title_full Two new cysteine endopeptidases obtained from the latex of Araujia hortorum fruits
title_fullStr Two new cysteine endopeptidases obtained from the latex of Araujia hortorum fruits
title_full_unstemmed Two new cysteine endopeptidases obtained from the latex of Araujia hortorum fruits
title_sort Two new cysteine endopeptidases obtained from the latex of Araujia hortorum fruits
dc.creator.none.fl_str_mv Obregón, Walter David
Arribére, María Cecilia
Morcelle del Valle, Susana Raquel
Liggieri, Constanza Silvina
Caffini, Néstor Oscar
Priolo de Lufrano, Nora Silvia
author Obregón, Walter David
author_facet Obregón, Walter David
Arribére, María Cecilia
Morcelle del Valle, Susana Raquel
Liggieri, Constanza Silvina
Caffini, Néstor Oscar
Priolo de Lufrano, Nora Silvia
author_role author
author2 Arribére, María Cecilia
Morcelle del Valle, Susana Raquel
Liggieri, Constanza Silvina
Caffini, Néstor Oscar
Priolo de Lufrano, Nora Silvia
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Química
Araujiain
Cysteine endopeptidases
Latex
Milkweed family
Protein purification
topic Química
Araujiain
Cysteine endopeptidases
Latex
Milkweed family
Protein purification
dc.description.none.fl_txt_mv Two new endopeptidases were purified to homogeneity from the latex of Araujia hortorum fruits by a simple purification procedure involving ultracentrifugation and ion exchange chromatography. Molecular weights of araujiain h II and araujiain h III were 23,718 and 23546 (mass spectrometry), respectively. The isoelectric point of araujiain h II was 8.9, whereas araujiain h III had a pI higher than 9.3. Maximum proteolytic activity on caseine was reached at pH 8.0-9.0 for both endopeptidases, which were irreversibly inhibited by iodoacetate and E-64, suggesting they belong to the cysteine protease family. Esterolytic activity was determined on N-alpha-CBZ-amino acid-p-nitrophenyl esters, and the highest kcat/Km values for the both enzymes were obtained with the glutamine derivative. The N-terminal sequences of araujiain h II and araujiain h III showed a high degree of homology with other plant cysteine endopeptidases.
Centro de Investigación de Proteínas Vegetales
description Two new endopeptidases were purified to homogeneity from the latex of Araujia hortorum fruits by a simple purification procedure involving ultracentrifugation and ion exchange chromatography. Molecular weights of araujiain h II and araujiain h III were 23,718 and 23546 (mass spectrometry), respectively. The isoelectric point of araujiain h II was 8.9, whereas araujiain h III had a pI higher than 9.3. Maximum proteolytic activity on caseine was reached at pH 8.0-9.0 for both endopeptidases, which were irreversibly inhibited by iodoacetate and E-64, suggesting they belong to the cysteine protease family. Esterolytic activity was determined on N-alpha-CBZ-amino acid-p-nitrophenyl esters, and the highest kcat/Km values for the both enzymes were obtained with the glutamine derivative. The N-terminal sequences of araujiain h II and araujiain h III showed a high degree of homology with other plant cysteine endopeptidases.
publishDate 2001
dc.date.none.fl_str_mv 2001
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/10915/143564
url http://sedici.unlp.edu.ar/handle/10915/143564
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:1010953718679
info:eu-repo/semantics/altIdentifier/pmid/11594466
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
317-325
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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score 13.070432

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