Isolation and Characterization of a Cysteine Protease from the Latex of <i>Araujia hortorum</i> Fruits

A new protease (<i>araujiain h l</i>) was purified to mass spectroscopy homogeneity from the latex of Araujia hortorum Fourn. (Asclepiadaceae) fruits by ultracentrifugation and ion exchange chromatography. The enzyme has a molecular mass of 24,031 (mass spectrometry) and an isoelectric p...

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Detalles Bibliográficos
Autores principales: Priolo de Lufrano, Nora Silvia, Morcelle del Valle, Susana Raquel, Arribére, María Cecilia, López, Laura María Isabel, Caffini, Néstor Oscar
Formato: Articulo
Lenguaje:Inglés
Publicado: 2000
Materias:
Biología
Araujia hortorum
Asclepiadaceae
latex
milkweed
plant proteases
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/138954
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-138954
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
Araujia hortorum
Asclepiadaceae
latex
milkweed
plant proteases
spellingShingle Biología
Araujia hortorum
Asclepiadaceae
latex
milkweed
plant proteases
Priolo de Lufrano, Nora Silvia
Morcelle del Valle, Susana Raquel
Arribére, María Cecilia
López, Laura María Isabel
Caffini, Néstor Oscar
Isolation and Characterization of a Cysteine Protease from the Latex of <i>Araujia hortorum</i> Fruits
topic_facet Biología
Araujia hortorum
Asclepiadaceae
latex
milkweed
plant proteases
description A new protease (<i>araujiain h l</i>) was purified to mass spectroscopy homogeneity from the latex of Araujia hortorum Fourn. (Asclepiadaceae) fruits by ultracentrifugation and ion exchange chromatography. The enzyme has a molecular mass of 24,031 (mass spectrometry) and an isoelectric point higher than 9.3. The optimum pH range for casein hydrolysis was 8.0–9.5. The enzyme showed remarkable caseinolytic activity at high temperatures, although its thermal stability decayed rapidly. The proteinase was activated by thiol compounds and inhibited by common thiol-blocking reagents, particularly E-64 and HgCl₂, suggesting the enzyme belongs to the cysteine protease family. The concentration of active sites as determined by titration with E-64 was 3.3 μM. When assayed on N-α-CBZ-amino acid-p-nitrophenyl esters, the enzyme showed higher preference for the glutamine derivative, followed by those of alanine, asparagine, glycine, and leucine, in decreasing order. Partial homology (36–48%) with other plant cysteine proteinases was observed in an internal fragment obtained by Protease V8 treatment.
format Articulo
Articulo
author Priolo de Lufrano, Nora Silvia
Morcelle del Valle, Susana Raquel
Arribére, María Cecilia
López, Laura María Isabel
Caffini, Néstor Oscar
author_facet Priolo de Lufrano, Nora Silvia
Morcelle del Valle, Susana Raquel
Arribére, María Cecilia
López, Laura María Isabel
Caffini, Néstor Oscar
author_sort Priolo de Lufrano, Nora Silvia
title Isolation and Characterization of a Cysteine Protease from the Latex of <i>Araujia hortorum</i> Fruits
title_short Isolation and Characterization of a Cysteine Protease from the Latex of <i>Araujia hortorum</i> Fruits
title_full Isolation and Characterization of a Cysteine Protease from the Latex of <i>Araujia hortorum</i> Fruits
title_fullStr Isolation and Characterization of a Cysteine Protease from the Latex of <i>Araujia hortorum</i> Fruits
title_full_unstemmed Isolation and Characterization of a Cysteine Protease from the Latex of <i>Araujia hortorum</i> Fruits
title_sort isolation and characterization of a cysteine protease from the latex of <i>araujia hortorum</i> fruits
publishDate 2000
url http://sedici.unlp.edu.ar/handle/10915/138954
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