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

Autores
Bruno, Mariela Anahí; Pardo, Marcelo Fabián; Caffini, Néstor Oscar; López, Laura María Isabel
Año de publicación
2003
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Centro de Investigación de Proteínas Vegetales
Materia
Biología
Bromelia hieronymi
Bromeliaceae
plant peptidases
cysteine proteinase
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/141355
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/141355
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Hieronymain I, a New Cysteine Peptidase Isolated from Unripe Fruits of <i>Bromelia hieronymi</i> Mez (Bromeliaceae)Bruno, Mariela AnahíPardo, Marcelo FabiánCaffini, Néstor OscarLópez, Laura María IsabelBiologíaBromelia hieronymiBromeliaceaeplant peptidasescysteine proteinaseA 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.Centro de Investigación de Proteínas Vegetales2003info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf127-134http://sedici.unlp.edu.ar/handle/10915/141355enginfo:eu-repo/semantics/altIdentifier/issn/0277-8033info:eu-repo/semantics/altIdentifier/issn/1573-4943info:eu-repo/semantics/altIdentifier/doi/10.1023/a:1023418812832info:eu-repo/semantics/altIdentifier/pmid/12760417info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T11:04:04Zoai:sedici.unlp.edu.ar:10915/141355Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 11:04:04.751SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Hieronymain I, a New Cysteine Peptidase Isolated from Unripe Fruits of <i>Bromelia hieronymi</i> Mez (Bromeliaceae)
title Hieronymain I, a New Cysteine Peptidase Isolated from Unripe Fruits of <i>Bromelia hieronymi</i> Mez (Bromeliaceae)
spellingShingle Hieronymain I, a New Cysteine Peptidase Isolated from Unripe Fruits of <i>Bromelia hieronymi</i> Mez (Bromeliaceae)
Bruno, Mariela Anahí
Biología
Bromelia hieronymi
Bromeliaceae
plant peptidases
cysteine proteinase
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)
dc.creator.none.fl_str_mv Bruno, Mariela Anahí
Pardo, Marcelo Fabián
Caffini, Néstor Oscar
López, Laura María Isabel
author Bruno, Mariela Anahí
author_facet Bruno, Mariela Anahí
Pardo, Marcelo Fabián
Caffini, Néstor Oscar
López, Laura María Isabel
author_role author
author2 Pardo, Marcelo Fabián
Caffini, Néstor Oscar
López, Laura María Isabel
author2_role author
author
author
dc.subject.none.fl_str_mv Biología
Bromelia hieronymi
Bromeliaceae
plant peptidases
cysteine proteinase
topic Biología
Bromelia hieronymi
Bromeliaceae
plant peptidases
cysteine proteinase
dc.description.none.fl_txt_mv 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.
Centro de Investigación de Proteínas Vegetales
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.
publishDate 2003
dc.date.none.fl_str_mv 2003
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/141355
url http://sedici.unlp.edu.ar/handle/10915/141355
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0277-8033
info:eu-repo/semantics/altIdentifier/issn/1573-4943
info:eu-repo/semantics/altIdentifier/doi/10.1023/a:1023418812832
info:eu-repo/semantics/altIdentifier/pmid/12760417
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
127-134
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.13397

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