Isolation and characterization of a myotoxin from Bothrops brazili Hoge, 1953 Hoge, 1953 snake venom (Ophidia: Viperidae).
A myotoxin from the venom of the snake Bothrops brazili has been purified by ion-exchange chromatography on CM-Sephadex C-50 with 0,05 M ammonium acetate buffer pH 7. The homogeneity was evaluated by PAGE with and without SDS, immunodiffusion and immunoelectrophoresis. The myotoxin is a basic protein with 15,6% of Lys+Arg; it is not a glicoprotein, has not enzymatic activity, and corresponds to 25% of the whole venom protein. The molecular weight of the myotoxin was determined by PAGE-SDS and gel filtration chromatography. The myotoxin has 30 KDa of molecular weight and two polypeptide chains of 15 KDa each. Myotoxin produces a severe necrosis on the gastrocnemius muscle of white mice. The myotoxin does not have hemolytic nor anticoagulant activity. However, produces edema with a DEM of 32,6 mg of protein.
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Universidad Nacional Mayor de San Marcos, Facultad de Ciencias Biológicas
2001
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oai:ojs.csi.unmsm:article67162020-05-25T23:38:28Z Isolation and characterization of a myotoxin from Bothrops brazili Hoge, 1953 Hoge, 1953 snake venom (Ophidia: Viperidae). Aislamiento y caracterización de una miotoxina del veneno de la serpiente Bothrops brazili Hoge, 1953 (Ophidia: Viperidae) Pantigoso, Carmen Escobar, Enrique Yarlequé, Armando myotoxin Bothrops brazili snake venom myonecrosis. miotoxina Bothrops brazili veneno de serpiente mionecrosis. A myotoxin from the venom of the snake Bothrops brazili has been purified by ion-exchange chromatography on CM-Sephadex C-50 with 0,05 M ammonium acetate buffer pH 7. The homogeneity was evaluated by PAGE with and without SDS, immunodiffusion and immunoelectrophoresis. The myotoxin is a basic protein with 15,6% of Lys+Arg; it is not a glicoprotein, has not enzymatic activity, and corresponds to 25% of the whole venom protein. The molecular weight of the myotoxin was determined by PAGE-SDS and gel filtration chromatography. The myotoxin has 30 KDa of molecular weight and two polypeptide chains of 15 KDa each. Myotoxin produces a severe necrosis on the gastrocnemius muscle of white mice. The myotoxin does not have hemolytic nor anticoagulant activity. However, produces edema with a DEM of 32,6 mg of protein. Se ha purificado una miotoxina del veneno de la serpiente Bothrops brazili, empleando un solo paso cromatográfico de intercambio iónico sobre CM-Sephadex C-50 con buffer acetato de amonio 0,05 M pH 7. La pureza de la proteína fue evaluada por PAGE con y sin SDS, inmunodifusión e inmunoelectroforesis. La proteína es de naturaleza básica y contiene 15,6% de Lys+Arg; además, no está glicosilada, carece de actividad enzimática, y por el método de Lowry se ha calculado que ella constituye el 25% de la proteína total del veneno. Por PAGE-SDS y cromatografía de filtración, se ha determinado que la miotoxina tiene un peso molecular de 30 KDa, y está formada por 2 cadenas polipeptídicas de 15 KDa cada una. La inoculación de la miotoxina en el músculo gastrocnemius de ratones albinos, produce una severa necrosis del tejido. La miotoxina no tiene actividad hemolítica ni anticoagulante; sin embargo, sí produce edema, se ha calculado una DEM de 32,6 mg de proteína. Universidad Nacional Mayor de San Marcos, Facultad de Ciencias Biológicas 2001-12-31 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/article info:eu-repo/semantics/article application/pdf https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/6716 10.15381/rpb.v8i2.6716 Revista Peruana de Biología; Vol. 8 No. 2 (2001); 136 -148 Revista Peruana de Biología; Vol. 8 Núm. 2 (2001); 136 -148 1727-9933 1561-0837 spa https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/6716/5962 Derechos de autor 2001 Carmen Pantigoso, Enrique Escobar, Armando Yarlequé https://creativecommons.org/licenses/by-nc-sa/4.0 |
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Biblioteca de la Facultad de Ciencias Biológicas |
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Digital |
| author |
Pantigoso, Carmen Escobar, Enrique Yarlequé, Armando |
| spellingShingle |
Pantigoso, Carmen Escobar, Enrique Yarlequé, Armando Isolation and characterization of a myotoxin from Bothrops brazili Hoge, 1953 Hoge, 1953 snake venom (Ophidia: Viperidae). |
| author_facet |
Pantigoso, Carmen Escobar, Enrique Yarlequé, Armando |
| author_sort |
Pantigoso, Carmen |
| title |
Isolation and characterization of a myotoxin from Bothrops brazili Hoge, 1953 Hoge, 1953 snake venom (Ophidia: Viperidae). |
| title_short |
Isolation and characterization of a myotoxin from Bothrops brazili Hoge, 1953 Hoge, 1953 snake venom (Ophidia: Viperidae). |
| title_full |
Isolation and characterization of a myotoxin from Bothrops brazili Hoge, 1953 Hoge, 1953 snake venom (Ophidia: Viperidae). |
| title_fullStr |
Isolation and characterization of a myotoxin from Bothrops brazili Hoge, 1953 Hoge, 1953 snake venom (Ophidia: Viperidae). |
| title_full_unstemmed |
Isolation and characterization of a myotoxin from Bothrops brazili Hoge, 1953 Hoge, 1953 snake venom (Ophidia: Viperidae). |
| title_sort |
isolation and characterization of a myotoxin from bothrops brazili hoge, 1953 hoge, 1953 snake venom (ophidia: viperidae). |
| description |
A myotoxin from the venom of the snake Bothrops brazili has been purified by ion-exchange chromatography on CM-Sephadex C-50 with 0,05 M ammonium acetate buffer pH 7. The homogeneity was evaluated by PAGE with and without SDS, immunodiffusion and immunoelectrophoresis. The myotoxin is a basic protein with 15,6% of Lys+Arg; it is not a glicoprotein, has not enzymatic activity, and corresponds to 25% of the whole venom protein. The molecular weight of the myotoxin was determined by PAGE-SDS and gel filtration chromatography. The myotoxin has 30 KDa of molecular weight and two polypeptide chains of 15 KDa each. Myotoxin produces a severe necrosis on the gastrocnemius muscle of white mice. The myotoxin does not have hemolytic nor anticoagulant activity. However, produces edema with a DEM of 32,6 mg of protein. |
| publisher |
Universidad Nacional Mayor de San Marcos, Facultad de Ciencias Biológicas |
| publishDate |
2001 |
| url |
https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/6716 |
| work_keys_str_mv |
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