Funastrain c II: A Cysteine Endopeptidase Purified from the Latex of <i>Funastrum clausum</i>

A cysteine endopeptidase, named funastrain c II, was isolated and characterized from the latex of Funastrum clausum (Asclepiadaceae). The molecular mass (mass spectrometry) of the protease was 23.636 kDa. The analysis of funastrain c II by SDS-PAGE revealed a single polypeptide chain. The enzyme sho...

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Detalles Bibliográficos
Autores principales: Morcelle del Valle, Susana Raquel, Trejo, Sebastián Alejandro, Canals, Francesc, Avilés, Francesc X., Priolo de Lufrano, Nora Silvia
Formato: Articulo
Lenguaje:Inglés
Publicado: 2004
Materias:
Biología
Cysteine endopeptidases
<i>Funastrum clausum</i>
Latex
Plant proteases
Protein purification
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/97753
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-97753
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
Cysteine endopeptidases
<i>Funastrum clausum</i>
Latex
Plant proteases
Protein purification
spellingShingle Biología
Cysteine endopeptidases
<i>Funastrum clausum</i>
Latex
Plant proteases
Protein purification
Morcelle del Valle, Susana Raquel
Trejo, Sebastián Alejandro
Canals, Francesc
Avilés, Francesc X.
Priolo de Lufrano, Nora Silvia
Funastrain c II: A Cysteine Endopeptidase Purified from the Latex of <i>Funastrum clausum</i>
topic_facet Biología
Cysteine endopeptidases
<i>Funastrum clausum</i>
Latex
Plant proteases
Protein purification
description A cysteine endopeptidase, named funastrain c II, was isolated and characterized from the latex of Funastrum clausum (Asclepiadaceae). The molecular mass (mass spectrometry) of the protease was 23.636 kDa. The analysis of funastrain c II by SDS-PAGE revealed a single polypeptide chain. The enzyme showed a remarkable stability of its caseinolytic activity after incubation at temperatures as high as 70°C. Inhibition and activation assays indicated the cysteinic nature of the funastrain c II catalytic site. The optimum pH of funastrain c II enzymatic activity varied according to the substrate used (9.0–10.0 for casein and 6.2–6.8 for PFLNA). Kinetic parameters were determined for N-α-CBZ-Ala p-nitrophenyl ester (Km = 0.0243 mM, kcat = 1.5 s–1) and L-pyroglutamyl-L-phenylalanyl-L-leucine-p-nitroanilide (PFLNA; KM = 0.1011 mM, kcat = 0.9 s–1). The N-terminal sequence of funastrain c II showed considerable similarity to other proteases isolated from latex of different Asclepiadaceae species as well as to other cysteine proteinases belonging to the papain family.
format Articulo
Articulo
author Morcelle del Valle, Susana Raquel
Trejo, Sebastián Alejandro
Canals, Francesc
Avilés, Francesc X.
Priolo de Lufrano, Nora Silvia
author_facet Morcelle del Valle, Susana Raquel
Trejo, Sebastián Alejandro
Canals, Francesc
Avilés, Francesc X.
Priolo de Lufrano, Nora Silvia
author_sort Morcelle del Valle, Susana Raquel
title Funastrain c II: A Cysteine Endopeptidase Purified from the Latex of <i>Funastrum clausum</i>
title_short Funastrain c II: A Cysteine Endopeptidase Purified from the Latex of <i>Funastrum clausum</i>
title_full Funastrain c II: A Cysteine Endopeptidase Purified from the Latex of <i>Funastrum clausum</i>
title_fullStr Funastrain c II: A Cysteine Endopeptidase Purified from the Latex of <i>Funastrum clausum</i>
title_full_unstemmed Funastrain c II: A Cysteine Endopeptidase Purified from the Latex of <i>Funastrum clausum</i>
title_sort funastrain c ii: a cysteine endopeptidase purified from the latex of <i>funastrum clausum</i>
publishDate 2004
url http://sedici.unlp.edu.ar/handle/10915/97753
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