Biochemical and PMF MALDI-TOF analyses of two novel papain-like plant proteinases

Two cysteine endopeptidases from latex of Araujia angustifolia (araujiain aI and araujiain aIII) were purified and characterized by means of conventional and proteomics techniques (MALDI-TOF). N-terminal sequences showed a high percentage of identity with cysteine proteinases belonging to the papain...

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Autores principales: Obregón, Walter David, Liggieri, Constanza Silvina, Morcelle del Valle, Susana Raquel, Trejo, S. A., Avilés, F. X., Priolo de Lufrano, Nora Silvia
Formato: Articulo
Lenguaje:Inglés
Publicado: 2009
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Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/153066
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id I19-R120-10915-153066
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spelling I19-R120-10915-1530662023-05-17T04:06:03Z http://sedici.unlp.edu.ar/handle/10915/153066 issn:1875-5305 Biochemical and PMF MALDI-TOF analyses of two novel papain-like plant proteinases Obregón, Walter David Liggieri, Constanza Silvina Morcelle del Valle, Susana Raquel Trejo, S. A. Avilés, F. X. Priolo de Lufrano, Nora Silvia 2009 2023-05-16T14:34:23Z en Biología Plant proteinases Asclepiadaceae Araujia angustifolia Peptide mass fingerprint Proteomics techniques Two cysteine endopeptidases from latex of Araujia angustifolia (araujiain aI and araujiain aIII) were purified and characterized by means of conventional and proteomics techniques (MALDI-TOF). N-terminal sequences showed a high percentage of identity with cysteine proteinases belonging to the papain family. The peptide mass fingerprint analysis demonstrated a close homology among both proteinases. Centro de Investigación de Proteínas Vegetales Articulo Articulo http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) application/pdf
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
Plant proteinases
Asclepiadaceae
Araujia angustifolia
Peptide mass fingerprint
Proteomics techniques
spellingShingle Biología
Plant proteinases
Asclepiadaceae
Araujia angustifolia
Peptide mass fingerprint
Proteomics techniques
Obregón, Walter David
Liggieri, Constanza Silvina
Morcelle del Valle, Susana Raquel
Trejo, S. A.
Avilés, F. X.
Priolo de Lufrano, Nora Silvia
Biochemical and PMF MALDI-TOF analyses of two novel papain-like plant proteinases
topic_facet Biología
Plant proteinases
Asclepiadaceae
Araujia angustifolia
Peptide mass fingerprint
Proteomics techniques
description Two cysteine endopeptidases from latex of Araujia angustifolia (araujiain aI and araujiain aIII) were purified and characterized by means of conventional and proteomics techniques (MALDI-TOF). N-terminal sequences showed a high percentage of identity with cysteine proteinases belonging to the papain family. The peptide mass fingerprint analysis demonstrated a close homology among both proteinases.
format Articulo
Articulo
author Obregón, Walter David
Liggieri, Constanza Silvina
Morcelle del Valle, Susana Raquel
Trejo, S. A.
Avilés, F. X.
Priolo de Lufrano, Nora Silvia
author_facet Obregón, Walter David
Liggieri, Constanza Silvina
Morcelle del Valle, Susana Raquel
Trejo, S. A.
Avilés, F. X.
Priolo de Lufrano, Nora Silvia
author_sort Obregón, Walter David
title Biochemical and PMF MALDI-TOF analyses of two novel papain-like plant proteinases
title_short Biochemical and PMF MALDI-TOF analyses of two novel papain-like plant proteinases
title_full Biochemical and PMF MALDI-TOF analyses of two novel papain-like plant proteinases
title_fullStr Biochemical and PMF MALDI-TOF analyses of two novel papain-like plant proteinases
title_full_unstemmed Biochemical and PMF MALDI-TOF analyses of two novel papain-like plant proteinases
title_sort biochemical and pmf maldi-tof analyses of two novel papain-like plant proteinases
publishDate 2009
url http://sedici.unlp.edu.ar/handle/10915/153066
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