Thiol groups of soybean callus succinyl CoA synthetase
- Autores
- De Xifra, E.A.W.; Del C. Batlle, A.M.
- Año de publicación
- 1974
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- 1. 1. The reaction between 5,5′-dithio-bis-(2-nitrobenzoic acid) (DTNB) and the SH groups of soybean callus succinyl-CoA synthetase has been investigated. At pH 8-6 and 25° C, four SH groups are titrable with DTNB in the native enzyme. No additional thiol groups have been revealed after unfolding of the protein with 8 M urea. 2. 2. The loss of enzymatic activity paralleled the decrease in the number of free SH groups. As with p-mercuribenzoate and other mercurials, reaction with DTNB also resulted in dissociation of the enzyme into subunits. © 1974.
Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. - Fuente
- Int. J. Biochem. 1974;5(2):129-135
- Materia
-
5
5′-dithio-bis-(2-nitrobenzoic acid)
enzyme inactivation
kinetics
molecular weight changes
soybean callus tissue
subunits
Succinyl-CoA synthetase
thiol groups - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by/2.5/ar
- Repositorio
.jpg)
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_0020711X_v5_n2_p129_DeXifra
Ver los metadatos del registro completo
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Thiol groups of soybean callus succinyl CoA synthetaseDe Xifra, E.A.W.Del C. Batlle, A.M.55′-dithio-bis-(2-nitrobenzoic acid)enzyme inactivationkineticsmolecular weight changessoybean callus tissuesubunitsSuccinyl-CoA synthetasethiol groups1. 1. The reaction between 5,5′-dithio-bis-(2-nitrobenzoic acid) (DTNB) and the SH groups of soybean callus succinyl-CoA synthetase has been investigated. At pH 8-6 and 25° C, four SH groups are titrable with DTNB in the native enzyme. No additional thiol groups have been revealed after unfolding of the protein with 8 M urea. 2. 2. The loss of enzymatic activity paralleled the decrease in the number of free SH groups. As with p-mercuribenzoate and other mercurials, reaction with DTNB also resulted in dissociation of the enzyme into subunits. © 1974.Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.1974info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_0020711X_v5_n2_p129_DeXifraInt. J. Biochem. 1974;5(2):129-135reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-29T13:43:05Zpaperaa:paper_0020711X_v5_n2_p129_DeXifraInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:43:07.151Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse |
| dc.title.none.fl_str_mv |
Thiol groups of soybean callus succinyl CoA synthetase |
| title |
Thiol groups of soybean callus succinyl CoA synthetase |
| spellingShingle |
Thiol groups of soybean callus succinyl CoA synthetase De Xifra, E.A.W. 5 5′-dithio-bis-(2-nitrobenzoic acid) enzyme inactivation kinetics molecular weight changes soybean callus tissue subunits Succinyl-CoA synthetase thiol groups |
| title_short |
Thiol groups of soybean callus succinyl CoA synthetase |
| title_full |
Thiol groups of soybean callus succinyl CoA synthetase |
| title_fullStr |
Thiol groups of soybean callus succinyl CoA synthetase |
| title_full_unstemmed |
Thiol groups of soybean callus succinyl CoA synthetase |
| title_sort |
Thiol groups of soybean callus succinyl CoA synthetase |
| dc.creator.none.fl_str_mv |
De Xifra, E.A.W. Del C. Batlle, A.M. |
| author |
De Xifra, E.A.W. |
| author_facet |
De Xifra, E.A.W. Del C. Batlle, A.M. |
| author_role |
author |
| author2 |
Del C. Batlle, A.M. |
| author2_role |
author |
| dc.subject.none.fl_str_mv |
5 5′-dithio-bis-(2-nitrobenzoic acid) enzyme inactivation kinetics molecular weight changes soybean callus tissue subunits Succinyl-CoA synthetase thiol groups |
| topic |
5 5′-dithio-bis-(2-nitrobenzoic acid) enzyme inactivation kinetics molecular weight changes soybean callus tissue subunits Succinyl-CoA synthetase thiol groups |
| dc.description.none.fl_txt_mv |
1. 1. The reaction between 5,5′-dithio-bis-(2-nitrobenzoic acid) (DTNB) and the SH groups of soybean callus succinyl-CoA synthetase has been investigated. At pH 8-6 and 25° C, four SH groups are titrable with DTNB in the native enzyme. No additional thiol groups have been revealed after unfolding of the protein with 8 M urea. 2. 2. The loss of enzymatic activity paralleled the decrease in the number of free SH groups. As with p-mercuribenzoate and other mercurials, reaction with DTNB also resulted in dissociation of the enzyme into subunits. © 1974. Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. |
| description |
1. 1. The reaction between 5,5′-dithio-bis-(2-nitrobenzoic acid) (DTNB) and the SH groups of soybean callus succinyl-CoA synthetase has been investigated. At pH 8-6 and 25° C, four SH groups are titrable with DTNB in the native enzyme. No additional thiol groups have been revealed after unfolding of the protein with 8 M urea. 2. 2. The loss of enzymatic activity paralleled the decrease in the number of free SH groups. As with p-mercuribenzoate and other mercurials, reaction with DTNB also resulted in dissociation of the enzyme into subunits. © 1974. |
| publishDate |
1974 |
| dc.date.none.fl_str_mv |
1974 |
| 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/20.500.12110/paper_0020711X_v5_n2_p129_DeXifra |
| url |
http://hdl.handle.net/20.500.12110/paper_0020711X_v5_n2_p129_DeXifra |
| dc.language.none.fl_str_mv |
eng |
| language |
eng |
| dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar |
| eu_rights_str_mv |
openAccess |
| rights_invalid_str_mv |
http://creativecommons.org/licenses/by/2.5/ar |
| dc.format.none.fl_str_mv |
application/pdf |
| dc.source.none.fl_str_mv |
Int. J. Biochem. 1974;5(2):129-135 reponame:Biblioteca Digital (UBA-FCEN) instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales instacron:UBA-FCEN |
| reponame_str |
Biblioteca Digital (UBA-FCEN) |
| collection |
Biblioteca Digital (UBA-FCEN) |
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Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
| instacron_str |
UBA-FCEN |
| institution |
UBA-FCEN |
| repository.name.fl_str_mv |
Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
| repository.mail.fl_str_mv |
ana@bl.fcen.uba.ar |
| _version_ |
1844618739375407104 |
| score |
13.070432 |