Prorenins activation by an enzyme from rat plasma (PreR-Co)

Autores
Vincent, Paula Andrea; Adler, Conrado; Avila, Cesar Luis; Guardia, Dora Cecilia; de Vito, Eduardo
Año de publicación
2002
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The aim of the present research was to explore the capacity of PreR-Co to process prorenin purified from kidney and corpora lutea (CL) and to study its action on extrarenal tissues. The PreR-Co was obtained from plasma as a single electrophoretic band by (NH4)2SO4 precipitation, gel filtration, anti-rat albumin immunoaffinity, and ion-exchange chromatography. Prorenin free of renin was obtained after (NH4)2SO4 precipitation, gel filtration, and ion-exchange chromatography by a passage through an affinity gel of H-77 Sepharose. SDS-PAGE of supernatant and of acidic elution from gel, exhibited a single band of 43 kDa and 35 kDa, respectively; both recognized by the specific anti rat renin antibody. The isolated renin was not attacked by PreR-Co; on the contrary prorenin was completely activated. The product of PreR-Co-activated prorenin showed an analogous MW to that of renin and was recognized by the specific antibody. In addition to processing kidney prorenin, PreR-Co was able to cleave inactive renin from ovary, CL, uterus and adrenal gland homogenates. However, the amount of active renin generated from these tissues was lower than those produced by trypsin activation. PreR-Co is a good candidate for the role of the enzyme involved in tissues prorenin activation.
Fil: Vincent, Paula Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Adler, Conrado. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Avila, Cesar Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Guardia, Dora Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: de Vito, Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Materia
INACTIVE RENIN
KIDNEY
PRORENIN
PRORENIN CONVERTING ENZYMES
RENIN
RENIN ACTIVATION
RENIN-ANGIOTENSIN SYSTEM
TRYPSIN
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:11336/95118
Acceder
id CONICETDig_5f89a23fd91460c76fa917d7cf43dadb
oai_identifier_str oai:ri.conicet.gov.ar:11336/95118
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Prorenins activation by an enzyme from rat plasma (PreR-Co)Vincent, Paula AndreaAdler, ConradoAvila, Cesar LuisGuardia, Dora Ceciliade Vito, EduardoINACTIVE RENINKIDNEYPRORENINPRORENIN CONVERTING ENZYMESRENINRENIN ACTIVATIONRENIN-ANGIOTENSIN SYSTEMTRYPSINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The aim of the present research was to explore the capacity of PreR-Co to process prorenin purified from kidney and corpora lutea (CL) and to study its action on extrarenal tissues. The PreR-Co was obtained from plasma as a single electrophoretic band by (NH4)2SO4 precipitation, gel filtration, anti-rat albumin immunoaffinity, and ion-exchange chromatography. Prorenin free of renin was obtained after (NH4)2SO4 precipitation, gel filtration, and ion-exchange chromatography by a passage through an affinity gel of H-77 Sepharose. SDS-PAGE of supernatant and of acidic elution from gel, exhibited a single band of 43 kDa and 35 kDa, respectively; both recognized by the specific anti rat renin antibody. The isolated renin was not attacked by PreR-Co; on the contrary prorenin was completely activated. The product of PreR-Co-activated prorenin showed an analogous MW to that of renin and was recognized by the specific antibody. In addition to processing kidney prorenin, PreR-Co was able to cleave inactive renin from ovary, CL, uterus and adrenal gland homogenates. However, the amount of active renin generated from these tissues was lower than those produced by trypsin activation. PreR-Co is a good candidate for the role of the enzyme involved in tissues prorenin activation.Fil: Vincent, Paula Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Adler, Conrado. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Avila, Cesar Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Guardia, Dora Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: de Vito, Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaElsevier Science Inc2002-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/95118Vincent, Paula Andrea; Adler, Conrado; Avila, Cesar Luis; Guardia, Dora Cecilia; de Vito, Eduardo; Prorenins activation by an enzyme from rat plasma (PreR-Co); Elsevier Science Inc; Comparative Biochemistry And Physiology. Part B, Biochemistry & Molecular Biology.; 131; 2; 12-2002; 201-2071096-4959CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1096495901004948info:eu-repo/semantics/altIdentifier/doi/10.1016/S1096-4959(01)00494-8info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:53:06Zoai:ri.conicet.gov.ar:11336/95118instacron: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:34982025-09-03 09:53:06.798CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Prorenins activation by an enzyme from rat plasma (PreR-Co)
title Prorenins activation by an enzyme from rat plasma (PreR-Co)
spellingShingle Prorenins activation by an enzyme from rat plasma (PreR-Co)
Vincent, Paula Andrea
INACTIVE RENIN
KIDNEY
PRORENIN
PRORENIN CONVERTING ENZYMES
RENIN
RENIN ACTIVATION
RENIN-ANGIOTENSIN SYSTEM
TRYPSIN
title_short Prorenins activation by an enzyme from rat plasma (PreR-Co)
title_full Prorenins activation by an enzyme from rat plasma (PreR-Co)
title_fullStr Prorenins activation by an enzyme from rat plasma (PreR-Co)
title_full_unstemmed Prorenins activation by an enzyme from rat plasma (PreR-Co)
title_sort Prorenins activation by an enzyme from rat plasma (PreR-Co)
dc.creator.none.fl_str_mv Vincent, Paula Andrea
Adler, Conrado
Avila, Cesar Luis
Guardia, Dora Cecilia
de Vito, Eduardo
author Vincent, Paula Andrea
author_facet Vincent, Paula Andrea
Adler, Conrado
Avila, Cesar Luis
Guardia, Dora Cecilia
de Vito, Eduardo
author_role author
author2 Adler, Conrado
Avila, Cesar Luis
Guardia, Dora Cecilia
de Vito, Eduardo
author2_role author
author
author
author
dc.subject.none.fl_str_mv INACTIVE RENIN
KIDNEY
PRORENIN
PRORENIN CONVERTING ENZYMES
RENIN
RENIN ACTIVATION
RENIN-ANGIOTENSIN SYSTEM
TRYPSIN
topic INACTIVE RENIN
KIDNEY
PRORENIN
PRORENIN CONVERTING ENZYMES
RENIN
RENIN ACTIVATION
RENIN-ANGIOTENSIN SYSTEM
TRYPSIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The aim of the present research was to explore the capacity of PreR-Co to process prorenin purified from kidney and corpora lutea (CL) and to study its action on extrarenal tissues. The PreR-Co was obtained from plasma as a single electrophoretic band by (NH4)2SO4 precipitation, gel filtration, anti-rat albumin immunoaffinity, and ion-exchange chromatography. Prorenin free of renin was obtained after (NH4)2SO4 precipitation, gel filtration, and ion-exchange chromatography by a passage through an affinity gel of H-77 Sepharose. SDS-PAGE of supernatant and of acidic elution from gel, exhibited a single band of 43 kDa and 35 kDa, respectively; both recognized by the specific anti rat renin antibody. The isolated renin was not attacked by PreR-Co; on the contrary prorenin was completely activated. The product of PreR-Co-activated prorenin showed an analogous MW to that of renin and was recognized by the specific antibody. In addition to processing kidney prorenin, PreR-Co was able to cleave inactive renin from ovary, CL, uterus and adrenal gland homogenates. However, the amount of active renin generated from these tissues was lower than those produced by trypsin activation. PreR-Co is a good candidate for the role of the enzyme involved in tissues prorenin activation.
Fil: Vincent, Paula Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Adler, Conrado. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Avila, Cesar Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Guardia, Dora Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: de Vito, Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
description The aim of the present research was to explore the capacity of PreR-Co to process prorenin purified from kidney and corpora lutea (CL) and to study its action on extrarenal tissues. The PreR-Co was obtained from plasma as a single electrophoretic band by (NH4)2SO4 precipitation, gel filtration, anti-rat albumin immunoaffinity, and ion-exchange chromatography. Prorenin free of renin was obtained after (NH4)2SO4 precipitation, gel filtration, and ion-exchange chromatography by a passage through an affinity gel of H-77 Sepharose. SDS-PAGE of supernatant and of acidic elution from gel, exhibited a single band of 43 kDa and 35 kDa, respectively; both recognized by the specific anti rat renin antibody. The isolated renin was not attacked by PreR-Co; on the contrary prorenin was completely activated. The product of PreR-Co-activated prorenin showed an analogous MW to that of renin and was recognized by the specific antibody. In addition to processing kidney prorenin, PreR-Co was able to cleave inactive renin from ovary, CL, uterus and adrenal gland homogenates. However, the amount of active renin generated from these tissues was lower than those produced by trypsin activation. PreR-Co is a good candidate for the role of the enzyme involved in tissues prorenin activation.
publishDate 2002
dc.date.none.fl_str_mv 2002-12
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/11336/95118
Vincent, Paula Andrea; Adler, Conrado; Avila, Cesar Luis; Guardia, Dora Cecilia; de Vito, Eduardo; Prorenins activation by an enzyme from rat plasma (PreR-Co); Elsevier Science Inc; Comparative Biochemistry And Physiology. Part B, Biochemistry & Molecular Biology.; 131; 2; 12-2002; 201-207
1096-4959
CONICET Digital
CONICET
url http://hdl.handle.net/11336/95118
identifier_str_mv Vincent, Paula Andrea; Adler, Conrado; Avila, Cesar Luis; Guardia, Dora Cecilia; de Vito, Eduardo; Prorenins activation by an enzyme from rat plasma (PreR-Co); Elsevier Science Inc; Comparative Biochemistry And Physiology. Part B, Biochemistry & Molecular Biology.; 131; 2; 12-2002; 201-207
1096-4959
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.sciencedirect.com/science/article/pii/S1096495901004948
info:eu-repo/semantics/altIdentifier/doi/10.1016/S1096-4959(01)00494-8
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science Inc
publisher.none.fl_str_mv Elsevier Science Inc
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
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score 13.13397

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