Purification and characterization of amino acid oxidase l-snake venom Bothrops Brazili “Jergón Shushupe"
Descripción del Articulo
An L-aminoacid oxidase was purified from Bothrops brazili snake venom using Sephadex G-100 and CM-Sepahdex C?50 chromatographic method; in both cases 0,1M ammonium acetate pH 6 was used as a eluted. The enzyme was purified 29,3 fold with 30,9% of yield. A homogeneus protein band was achieved by PAGE...
| Autores: | , , , |
|---|---|
| Formato: | artículo |
| Fecha de Publicación: | 1999 |
| Institución: | Universidad Nacional Mayor de San Marcos |
| Repositorio: | Revistas - Universidad Nacional Mayor de San Marcos |
| Lenguaje: | español |
| OAI Identifier: | oai:ojs.csi.unmsm:article/8302 |
| Enlace del recurso: | https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/8302 |
| Nivel de acceso: | acceso abierto |
| Materia: | L-aminoácido oxidasa Bothrops brazili veneno antibacteriano proteína. L-amino acid oxidase venom antibacterial protein. |
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Purification and characterization of amino acid oxidase l-snake venom Bothrops Brazili “Jergón Shushupe"Purificación y caracterización de la l-amino ácido oxidasa del veneno de la serpiente Bothrops brazili "jergón shushupe"Solís, ChristianEscobar, EnriqueYarlequé, ArmandoGutiérrez, SusanaL-aminoácido oxidasaBothrops brazilivenenoantibacterianoproteína.L-amino acid oxidaseBothrops brazilivenomantibacterialprotein.An L-aminoacid oxidase was purified from Bothrops brazili snake venom using Sephadex G-100 and CM-Sepahdex C?50 chromatographic method; in both cases 0,1M ammonium acetate pH 6 was used as a eluted. The enzyme was purified 29,3 fold with 30,9% of yield. A homogeneus protein band was achieved by PAGE-SDS, inmunodifusion as well as immunoelectrophoresis. The enzyme was an acid glicoprotein with a molecular weight of 125,7 kd consisting of two subunits of 59,91 kd each, linked by noncovalent bonds. The optimum pH was in the range of 7,5 to 9,0 depending on the L-aminoacid used as substrate. It was a thermoestable protein untill 55 oC, but its activity decreased by alcaline treatment. On the other hand, antibacterial assays using the Grove's method demonstrated that the whole venom as well as its purified enzyme produced a severe action on standardized grown cultures of Staphylococcus aureus, Vibrio cholerae and Streptococcus faecalis.Se ha purificado y caracterizado parcialmente la L-aminoácido oxidasa de la serpiente Bothrops brazili. El aislamiento se realizó usando técnicas cromatográficas en Sephadex G-100 y CM-Sephadex C-50, utilizando como eluyente buffer acetato de amonio 0,1M pH 6. La enzima fue purificada 29,3 veces con un rendimiento de 30,9%. Usando electroforesis en gel de poliacrilamida con dodecil sulfato de sodio (PAGE-SDS) en condiciones reductoras y no reductoras, así como las técnicas de inmunodifusión e inmunoelectroforesis, se demostró la presencia de una sola banda proteica. La enzima fue caracterizada como una glicoproteína ácida con un peso molecular de 125,7 kd formada por dos subunidades de 59,9 kd unidas por enlaces débiles, con un pH óptimo entre 7,5 y 9, dependiendo del aminoácido usado como substrato; siendo termoestable hasta los 550 C y lábil a pH alcalino. Asimismo, los ensayos por el método del cilindro en placa de Grove demostraron el efecto antibacteriano de la proteína aislada en cepas estandarizadas de Staphylococcus aureus, Vibrio cholerae y Streptococcus faecalis.Universidad Nacional Mayor de San Marcos, Facultad de Ciencias Biológicas1999-06-14info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/830210.15381/rpb.v6i1.8302Revista Peruana de Biología; Vol. 6 Núm. 1 (1999); 075 - 084Revista Peruana de Biología; Vol. 6 No. 1 (1999); 075 - 0841727-99331561-0837reponame:Revistas - Universidad Nacional Mayor de San Marcosinstname:Universidad Nacional Mayor de San Marcosinstacron:UNMSMspahttps://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/8302/7227Derechos de autor 1999 Christian Solís, Enrique Escobar, Armando Yarlequé, Susana Gutiérrezhttps://creativecommons.org/licenses/by-nc-sa/4.0info:eu-repo/semantics/openAccessoai:ojs.csi.unmsm:article/83022020-05-26T11:56:18Z |
| dc.title.none.fl_str_mv |
Purification and characterization of amino acid oxidase l-snake venom Bothrops Brazili “Jergón Shushupe" Purificación y caracterización de la l-amino ácido oxidasa del veneno de la serpiente Bothrops brazili "jergón shushupe" |
| title |
Purification and characterization of amino acid oxidase l-snake venom Bothrops Brazili “Jergón Shushupe" |
| spellingShingle |
Purification and characterization of amino acid oxidase l-snake venom Bothrops Brazili “Jergón Shushupe" Solís, Christian L-aminoácido oxidasa Bothrops brazili veneno antibacteriano proteína. L-amino acid oxidase Bothrops brazili venom antibacterial protein. |
| title_short |
Purification and characterization of amino acid oxidase l-snake venom Bothrops Brazili “Jergón Shushupe" |
| title_full |
Purification and characterization of amino acid oxidase l-snake venom Bothrops Brazili “Jergón Shushupe" |
| title_fullStr |
Purification and characterization of amino acid oxidase l-snake venom Bothrops Brazili “Jergón Shushupe" |
| title_full_unstemmed |
Purification and characterization of amino acid oxidase l-snake venom Bothrops Brazili “Jergón Shushupe" |
| title_sort |
Purification and characterization of amino acid oxidase l-snake venom Bothrops Brazili “Jergón Shushupe" |
| dc.creator.none.fl_str_mv |
Solís, Christian Escobar, Enrique Yarlequé, Armando Gutiérrez, Susana |
| author |
Solís, Christian |
| author_facet |
Solís, Christian Escobar, Enrique Yarlequé, Armando Gutiérrez, Susana |
| author_role |
author |
| author2 |
Escobar, Enrique Yarlequé, Armando Gutiérrez, Susana |
| author2_role |
author author author |
| dc.subject.none.fl_str_mv |
L-aminoácido oxidasa Bothrops brazili veneno antibacteriano proteína. L-amino acid oxidase Bothrops brazili venom antibacterial protein. |
| topic |
L-aminoácido oxidasa Bothrops brazili veneno antibacteriano proteína. L-amino acid oxidase Bothrops brazili venom antibacterial protein. |
| description |
An L-aminoacid oxidase was purified from Bothrops brazili snake venom using Sephadex G-100 and CM-Sepahdex C?50 chromatographic method; in both cases 0,1M ammonium acetate pH 6 was used as a eluted. The enzyme was purified 29,3 fold with 30,9% of yield. A homogeneus protein band was achieved by PAGE-SDS, inmunodifusion as well as immunoelectrophoresis. The enzyme was an acid glicoprotein with a molecular weight of 125,7 kd consisting of two subunits of 59,91 kd each, linked by noncovalent bonds. The optimum pH was in the range of 7,5 to 9,0 depending on the L-aminoacid used as substrate. It was a thermoestable protein untill 55 oC, but its activity decreased by alcaline treatment. On the other hand, antibacterial assays using the Grove's method demonstrated that the whole venom as well as its purified enzyme produced a severe action on standardized grown cultures of Staphylococcus aureus, Vibrio cholerae and Streptococcus faecalis. |
| publishDate |
1999 |
| dc.date.none.fl_str_mv |
1999-06-14 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
| format |
article |
| status_str |
publishedVersion |
| dc.identifier.none.fl_str_mv |
https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/8302 10.15381/rpb.v6i1.8302 |
| url |
https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/8302 |
| identifier_str_mv |
10.15381/rpb.v6i1.8302 |
| dc.language.none.fl_str_mv |
spa |
| language |
spa |
| dc.relation.none.fl_str_mv |
https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/8302/7227 |
| dc.rights.none.fl_str_mv |
Derechos de autor 1999 Christian Solís, Enrique Escobar, Armando Yarlequé, Susana Gutiérrez https://creativecommons.org/licenses/by-nc-sa/4.0 info:eu-repo/semantics/openAccess |
| rights_invalid_str_mv |
Derechos de autor 1999 Christian Solís, Enrique Escobar, Armando Yarlequé, Susana Gutiérrez https://creativecommons.org/licenses/by-nc-sa/4.0 |
| eu_rights_str_mv |
openAccess |
| dc.format.none.fl_str_mv |
application/pdf |
| dc.publisher.none.fl_str_mv |
Universidad Nacional Mayor de San Marcos, Facultad de Ciencias Biológicas |
| publisher.none.fl_str_mv |
Universidad Nacional Mayor de San Marcos, Facultad de Ciencias Biológicas |
| dc.source.none.fl_str_mv |
Revista Peruana de Biología; Vol. 6 Núm. 1 (1999); 075 - 084 Revista Peruana de Biología; Vol. 6 No. 1 (1999); 075 - 084 1727-9933 1561-0837 reponame:Revistas - Universidad Nacional Mayor de San Marcos instname:Universidad Nacional Mayor de San Marcos instacron:UNMSM |
| instname_str |
Universidad Nacional Mayor de San Marcos |
| instacron_str |
UNMSM |
| institution |
UNMSM |
| reponame_str |
Revistas - Universidad Nacional Mayor de San Marcos |
| collection |
Revistas - Universidad Nacional Mayor de San Marcos |
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| repository.mail.fl_str_mv |
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1795238310592905216 |
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13.958958 |
Nota importante:
La información contenida en este registro es de entera responsabilidad de la institución que gestiona el repositorio institucional donde esta contenido este documento o set de datos. El CONCYTEC no se hace responsable por los contenidos (publicaciones y/o datos) accesibles a través del Repositorio Nacional Digital de Ciencia, Tecnología e Innovación de Acceso Abierto (ALICIA).
La información contenida en este registro es de entera responsabilidad de la institución que gestiona el repositorio institucional donde esta contenido este documento o set de datos. El CONCYTEC no se hace responsable por los contenidos (publicaciones y/o datos) accesibles a través del Repositorio Nacional Digital de Ciencia, Tecnología e Innovación de Acceso Abierto (ALICIA).
