Characterization of the proteolytic system present in Vasconcellea quercifolia latex

Vasconcellea quercifolia (Caricaceae) latex contains several cysteine endopeptidases with high proteolytic activity. Cysteine endopeptidases are the main active compounds used by the plant as a defense mechanism. A proteolytic preparation from V. quercifolia (“o...

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Detalles Bibliográficos
Autores principales:	Figuerero Torres, María José, Trejo, Sebastián Alejandro, Obregón, Walter David, Avilés, Francesc Xavier, López, Laura María Isabel, Natalucci, Claudia Luisa
Formato:	Articulo
Lenguaje:	Inglés
Publicado:	2012
Materias:	Biología Caricaceae cDNA Cysteine endopeptidases Peptide mass fingerprint Plant proteases Vasconcellea
Acceso en línea:	http://sedici.unlp.edu.ar/handle/10915/132404
Aporte de:	SEDICI (UNLP) de Universidad Nacional de La Plata

id	I19-R120-10915-132404
record_format	dspace
institution	Universidad Nacional de La Plata
institution_str	I-19
repository_str	R-120
collection	SEDICI (UNLP)
language	Inglés
topic	Biología Caricaceae cDNA Cysteine endopeptidases Peptide mass fingerprint Plant proteases Vasconcellea
spellingShingle	Biología Caricaceae cDNA Cysteine endopeptidases Peptide mass fingerprint Plant proteases Vasconcellea Figuerero Torres, María José Trejo, Sebastián Alejandro Obregón, Walter David Avilés, Francesc Xavier López, Laura María Isabel Natalucci, Claudia Luisa Characterization of the proteolytic system present in <i>Vasconcellea quercifolia</i> latex
topic_facet	Biología Caricaceae cDNA Cysteine endopeptidases Peptide mass fingerprint Plant proteases Vasconcellea
description	<i>Vasconcellea quercifolia</i> (Caricaceae) latex contains several cysteine endopeptidases with high proteolytic activity. Cysteine endopeptidases are the main active compounds used by the plant as a defense mechanism. A proteolytic preparation from <i>V. quercifolia</i> (“oak leaved papaya”) latex was purified by cation exchange chromatography. From SDS-PAGE and blotting of the selected fractions, the N-terminal amino acid sequences of polypeptides were determined by Edman’s degradation. The analysis by peptide mass fingerprinting (PMF) of the enzymes allowed their characterization and confirmed the presence of seven different cysteine proteinases in the latex of <i>V. quercifolia</i>. Moreover, the comparison between the tryptic maps with those deposited in databases using the MASCOT tool showed that none of the isolated proteases matched with another plant protease. Notably, a propeptidase was detected in the plant latex, which is being the first report in this sense. Furthermore, the cDNA of one of the cysteine proteases that is expressed in the latex of <i>V. quercifolia</i> was cloned and sequenced. The consensus sequence was aligned using the ClustalX web server, which allowed detecting a high degree of identity with cysteine proteases of the Caricaceae family and establishing the evolutionary relationship between them. We also observed a high conservation degree for those amino acid residues which are essential for the catalytic activity and tridimensional structure of the plant proteases belonging to the subfamily C1A. The PMF analysis strongly suggests that the sequence obtained corresponds to the VQ-III peptidase.
format	Articulo Articulo
author	Figuerero Torres, María José Trejo, Sebastián Alejandro Obregón, Walter David Avilés, Francesc Xavier López, Laura María Isabel Natalucci, Claudia Luisa
author_facet	Figuerero Torres, María José Trejo, Sebastián Alejandro Obregón, Walter David Avilés, Francesc Xavier López, Laura María Isabel Natalucci, Claudia Luisa
author_sort	Figuerero Torres, María José
title	Characterization of the proteolytic system present in <i>Vasconcellea quercifolia</i> latex
title_short	Characterization of the proteolytic system present in <i>Vasconcellea quercifolia</i> latex
title_full	Characterization of the proteolytic system present in <i>Vasconcellea quercifolia</i> latex
title_fullStr	Characterization of the proteolytic system present in <i>Vasconcellea quercifolia</i> latex
title_full_unstemmed	Characterization of the proteolytic system present in <i>Vasconcellea quercifolia</i> latex
title_sort	characterization of the proteolytic system present in <i>vasconcellea quercifolia</i> latex
publishDate	2012
url	http://sedici.unlp.edu.ar/handle/10915/132404
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bdutipo_str	Repositorios
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Characterization of the proteolytic system present in <i>Vasconcellea quercifolia</i> latex

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