A Novel Trypsin and Chymotrypsin Inhibitor from Maclura pomifera Seeds

Autores
Lazza, Cristian Martin; Trejo, S.; Obregon, Walter David; Pistaccio, L.; Caffini, N.; Lopez, L.
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A new peptidic protease inhibitor (MpI) has been isolated from Maclura pomifera seeds, being the first trypsin and chymotrypsin inhibitor from a species belonging to the family Moraceae. MpI was purified by acetone precipitation, gel filtration and ion exchange chromatography, successively, with purification factors of 112 and 109 for the aforementioned enzymes, which are infrequent high values for inhibitors isolated from seeds. MpI showed a unique band in SDSTricine PAGE (Mr 11 kDa) and isoelectric focusing (pI = 5.2), inhibited the serine proteases trypsin and -chymotrypsin(IC50 0.17 and 0.7 μg/ml, respectively), but not cathepsin B (cysteine protease), cathepsin D (aspartic protease) nor carboxypeptidase A (metallo protease). The N-terminal sequence was determined (AREPKFSTHCEEEESR) but no homology was detected with other peptide inhibitors isolated from seeds. Preliminary assays related to blood clotting reactionsshowed that the isolated inhibitor significatively increased the activated partial thromboplastin time (APTT), suggesting its potential use in the treatment of blood coagulation disorders.
Fil: Lazza, Cristian Martin. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Trejo, S.. Universitat Autònoma de Barcelona; España
Fil: Obregon, Walter David. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Pistaccio, L.. Provincia de Buenos Aires. Ministerio de Salud. Hospital de Niños "Sor María Ludovica" de La Plata. Instituto de Desarrollo e Investigaciones Pediátricas; Argentina
Fil: Caffini, N.. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Lopez, L.. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Materia
Maclura pomifera seeds
Peptide trypsin inhibitor
Peptide chymotrypsin inhibitor
Moraceae
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/241241
Acceder
id CONICETDig_99f79a6f417d689d5f21a92cc9d70168
oai_identifier_str oai:ri.conicet.gov.ar:11336/241241
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A Novel Trypsin and Chymotrypsin Inhibitor from Maclura pomifera SeedsLazza, Cristian MartinTrejo, S.Obregon, Walter DavidPistaccio, L.Caffini, N.Lopez, L.Maclura pomifera seedsPeptide trypsin inhibitorPeptide chymotrypsin inhibitorMoraceaehttps://purl.org/becyt/ford/3.4https://purl.org/becyt/ford/3A new peptidic protease inhibitor (MpI) has been isolated from Maclura pomifera seeds, being the first trypsin and chymotrypsin inhibitor from a species belonging to the family Moraceae. MpI was purified by acetone precipitation, gel filtration and ion exchange chromatography, successively, with purification factors of 112 and 109 for the aforementioned enzymes, which are infrequent high values for inhibitors isolated from seeds. MpI showed a unique band in SDSTricine PAGE (Mr 11 kDa) and isoelectric focusing (pI = 5.2), inhibited the serine proteases trypsin and -chymotrypsin(IC50 0.17 and 0.7 μg/ml, respectively), but not cathepsin B (cysteine protease), cathepsin D (aspartic protease) nor carboxypeptidase A (metallo protease). The N-terminal sequence was determined (AREPKFSTHCEEEESR) but no homology was detected with other peptide inhibitors isolated from seeds. Preliminary assays related to blood clotting reactionsshowed that the isolated inhibitor significatively increased the activated partial thromboplastin time (APTT), suggesting its potential use in the treatment of blood coagulation disorders.Fil: Lazza, Cristian Martin. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Trejo, S.. Universitat Autònoma de Barcelona; EspañaFil: Obregon, Walter David. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Pistaccio, L.. Provincia de Buenos Aires. Ministerio de Salud. Hospital de Niños "Sor María Ludovica" de La Plata. Instituto de Desarrollo e Investigaciones Pediátricas; ArgentinaFil: Caffini, N.. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Lopez, L.. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaBentham Science Publishers2010-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/241241Lazza, Cristian Martin; Trejo, S.; Obregon, Walter David; Pistaccio, L.; Caffini, N.; et al.; A Novel Trypsin and Chymotrypsin Inhibitor from Maclura pomifera Seeds; Bentham Science Publishers; Letters In Drug Design & Discovery; 7; 4; 10-2010; 244-2491570-1808CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.eurekaselect.com/article/30941info:eu-repo/semantics/altIdentifier/doi/10.2174/157018010790945832info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:24:33Zoai:ri.conicet.gov.ar:11336/241241instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-10 13:24:33.903CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A Novel Trypsin and Chymotrypsin Inhibitor from Maclura pomifera Seeds
title A Novel Trypsin and Chymotrypsin Inhibitor from Maclura pomifera Seeds
spellingShingle A Novel Trypsin and Chymotrypsin Inhibitor from Maclura pomifera Seeds
Lazza, Cristian Martin
Maclura pomifera seeds
Peptide trypsin inhibitor
Peptide chymotrypsin inhibitor
Moraceae
title_short A Novel Trypsin and Chymotrypsin Inhibitor from Maclura pomifera Seeds
title_full A Novel Trypsin and Chymotrypsin Inhibitor from Maclura pomifera Seeds
title_fullStr A Novel Trypsin and Chymotrypsin Inhibitor from Maclura pomifera Seeds
title_full_unstemmed A Novel Trypsin and Chymotrypsin Inhibitor from Maclura pomifera Seeds
title_sort A Novel Trypsin and Chymotrypsin Inhibitor from Maclura pomifera Seeds
dc.creator.none.fl_str_mv Lazza, Cristian Martin
Trejo, S.
Obregon, Walter David
Pistaccio, L.
Caffini, N.
Lopez, L.
author Lazza, Cristian Martin
author_facet Lazza, Cristian Martin
Trejo, S.
Obregon, Walter David
Pistaccio, L.
Caffini, N.
Lopez, L.
author_role author
author2 Trejo, S.
Obregon, Walter David
Pistaccio, L.
Caffini, N.
Lopez, L.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Maclura pomifera seeds
Peptide trypsin inhibitor
Peptide chymotrypsin inhibitor
Moraceae
topic Maclura pomifera seeds
Peptide trypsin inhibitor
Peptide chymotrypsin inhibitor
Moraceae
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.4
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv A new peptidic protease inhibitor (MpI) has been isolated from Maclura pomifera seeds, being the first trypsin and chymotrypsin inhibitor from a species belonging to the family Moraceae. MpI was purified by acetone precipitation, gel filtration and ion exchange chromatography, successively, with purification factors of 112 and 109 for the aforementioned enzymes, which are infrequent high values for inhibitors isolated from seeds. MpI showed a unique band in SDSTricine PAGE (Mr 11 kDa) and isoelectric focusing (pI = 5.2), inhibited the serine proteases trypsin and -chymotrypsin(IC50 0.17 and 0.7 μg/ml, respectively), but not cathepsin B (cysteine protease), cathepsin D (aspartic protease) nor carboxypeptidase A (metallo protease). The N-terminal sequence was determined (AREPKFSTHCEEEESR) but no homology was detected with other peptide inhibitors isolated from seeds. Preliminary assays related to blood clotting reactionsshowed that the isolated inhibitor significatively increased the activated partial thromboplastin time (APTT), suggesting its potential use in the treatment of blood coagulation disorders.
Fil: Lazza, Cristian Martin. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Trejo, S.. Universitat Autònoma de Barcelona; España
Fil: Obregon, Walter David. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Pistaccio, L.. Provincia de Buenos Aires. Ministerio de Salud. Hospital de Niños "Sor María Ludovica" de La Plata. Instituto de Desarrollo e Investigaciones Pediátricas; Argentina
Fil: Caffini, N.. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Lopez, L.. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
description A new peptidic protease inhibitor (MpI) has been isolated from Maclura pomifera seeds, being the first trypsin and chymotrypsin inhibitor from a species belonging to the family Moraceae. MpI was purified by acetone precipitation, gel filtration and ion exchange chromatography, successively, with purification factors of 112 and 109 for the aforementioned enzymes, which are infrequent high values for inhibitors isolated from seeds. MpI showed a unique band in SDSTricine PAGE (Mr 11 kDa) and isoelectric focusing (pI = 5.2), inhibited the serine proteases trypsin and -chymotrypsin(IC50 0.17 and 0.7 μg/ml, respectively), but not cathepsin B (cysteine protease), cathepsin D (aspartic protease) nor carboxypeptidase A (metallo protease). The N-terminal sequence was determined (AREPKFSTHCEEEESR) but no homology was detected with other peptide inhibitors isolated from seeds. Preliminary assays related to blood clotting reactionsshowed that the isolated inhibitor significatively increased the activated partial thromboplastin time (APTT), suggesting its potential use in the treatment of blood coagulation disorders.
publishDate 2010
dc.date.none.fl_str_mv 2010-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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://hdl.handle.net/11336/241241
Lazza, Cristian Martin; Trejo, S.; Obregon, Walter David; Pistaccio, L.; Caffini, N.; et al.; A Novel Trypsin and Chymotrypsin Inhibitor from Maclura pomifera Seeds; Bentham Science Publishers; Letters In Drug Design & Discovery; 7; 4; 10-2010; 244-249
1570-1808
CONICET Digital
CONICET
url http://hdl.handle.net/11336/241241
identifier_str_mv Lazza, Cristian Martin; Trejo, S.; Obregon, Walter David; Pistaccio, L.; Caffini, N.; et al.; A Novel Trypsin and Chymotrypsin Inhibitor from Maclura pomifera Seeds; Bentham Science Publishers; Letters In Drug Design & Discovery; 7; 4; 10-2010; 244-249
1570-1808
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.eurekaselect.com/article/30941
info:eu-repo/semantics/altIdentifier/doi/10.2174/157018010790945832
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Bentham Science Publishers
publisher.none.fl_str_mv Bentham Science Publishers
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842981363351814144
score 12.493442

Publicaciones similares