Hieronymain I, a New Cysteine Peptidase Isolated from Unripe Fruits of <i>Bromelia hieronymi</i> Mez (Bromeliaceae)

A new peptidase, named hieronymain I, was purified to homogeneity from unripe fruits of Bromelia hieronymi Mez (Bromeliaceae) by acetone fractionation followed by cation exchange chromatography (FPLC) on CM-Sepharose FF. Homogeneity of the enzyme was confirmed by mass spectroscopy (MALDI-TOF), isoel...

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Detalles Bibliográficos
Autores principales: Bruno, Mariela Anahí, Pardo, Marcelo Fabián, Caffini, Néstor Oscar, López, Laura María Isabel
Formato: Articulo
Lenguaje:Inglés
Publicado: 2003
Materias:
Biología
Bromelia hieronymi
Bromeliaceae
plant peptidases
cysteine proteinase
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/141355
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-141355
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
Bromelia hieronymi
Bromeliaceae
plant peptidases
cysteine proteinase
spellingShingle Biología
Bromelia hieronymi
Bromeliaceae
plant peptidases
cysteine proteinase
Bruno, Mariela Anahí
Pardo, Marcelo Fabián
Caffini, Néstor Oscar
López, Laura María Isabel
Hieronymain I, a New Cysteine Peptidase Isolated from Unripe Fruits of <i>Bromelia hieronymi</i> Mez (Bromeliaceae)
topic_facet Biología
Bromelia hieronymi
Bromeliaceae
plant peptidases
cysteine proteinase
description A new peptidase, named hieronymain I, was purified to homogeneity from unripe fruits of Bromelia hieronymi Mez (Bromeliaceae) by acetone fractionation followed by cation exchange chromatography (FPLC) on CM-Sepharose FF. Homogeneity of the enzyme was confirmed by mass spectroscopy (MALDI-TOF), isoelectric focusing, and SDS-PAGE. Hieronymain is a basic peptidase (pI > 9.3) and its molecular mass was 24,066 Da. Maximum proteolytic activity on casein (>90% of maximum activity) was achieved at pH 8.5-9.5. The enzyme was completely inhibited by E-64 and iodoacetic acid and activated by the addition of cysteine; these results strongly suggest that the isolated protease should be included within the cysteine group. The N-terminal sequence of hieronymain (ALPESIDWRAKGAVTEVKRQDG) was compared with 25 plant cysteine proteases that showed more than 50% of identity.
format Articulo
Articulo
author Bruno, Mariela Anahí
Pardo, Marcelo Fabián
Caffini, Néstor Oscar
López, Laura María Isabel
author_facet Bruno, Mariela Anahí
Pardo, Marcelo Fabián
Caffini, Néstor Oscar
López, Laura María Isabel
author_sort Bruno, Mariela Anahí
title Hieronymain I, a New Cysteine Peptidase Isolated from Unripe Fruits of <i>Bromelia hieronymi</i> Mez (Bromeliaceae)
title_short Hieronymain I, a New Cysteine Peptidase Isolated from Unripe Fruits of <i>Bromelia hieronymi</i> Mez (Bromeliaceae)
title_full Hieronymain I, a New Cysteine Peptidase Isolated from Unripe Fruits of <i>Bromelia hieronymi</i> Mez (Bromeliaceae)
title_fullStr Hieronymain I, a New Cysteine Peptidase Isolated from Unripe Fruits of <i>Bromelia hieronymi</i> Mez (Bromeliaceae)
title_full_unstemmed Hieronymain I, a New Cysteine Peptidase Isolated from Unripe Fruits of <i>Bromelia hieronymi</i> Mez (Bromeliaceae)
title_sort hieronymain i, a new cysteine peptidase isolated from unripe fruits of <i>bromelia hieronymi</i> mez (bromeliaceae)
publishDate 2003
url http://sedici.unlp.edu.ar/handle/10915/141355
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AT caffininestoroscar hieronymainianewcysteinepeptidaseisolatedfromunripefruitsofibromeliahieronymiimezbromeliaceae
AT lopezlauramariaisabel hieronymainianewcysteinepeptidaseisolatedfromunripefruitsofibromeliahieronymiimezbromeliaceae
bdutipo_str Repositorios
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