PURIFICATION AND PARTIAL CHARACTERIZATION OF A GLYCOPROTEIN WITH AMIDOLYTIC ACTIVITY OBTAINED FROM SNAKE VENOM BOTHROPS BARNETTI
A glycoprotein from the venom of Bothrops barnetti snake , was purified using gel filtration and ionic exchange chromatography . This protein showed 48 kDa as molecular weight by PAGE-SDS under nonreducing conditions being its carbohydrate content 48% of the total mass protein. This enzyme had activ...
| Autores: | , , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2010 |
| País: | Perú |
| Institución: | Universidad Nacional Mayor de San Marcos |
| Repositorio: | Revistas - Universidad Nacional Mayor de San Marcos |
| Idioma: | español |
| OAI Identifier: | oai:revistasinvestigacion.unmsm.edu.pe:article/4600 |
| Acceso en línea: | https://revistasinvestigacion.unmsm.edu.pe/index.php/quim/article/view/4600 |
| Access Level: | acceso abierto |
| Palabra clave: | Venom snake amidolytic activity glycoprotein Bothrops barnetti Veneno serpiente actividad amidolítica glicoproteína |
| Sumario: | A glycoprotein from the venom of Bothrops barnetti snake , was purified using gel filtration and ionic exchange chromatography . This protein showed 48 kDa as molecular weight by PAGE-SDS under nonreducing conditions being its carbohydrate content 48% of the total mass protein. This enzyme had activity either Benzoil Arginil-p-Nitroanilide (BApNA) and human citrated plasma. In addition this enzyme was strongly inhibited by PMSF and tripsin soybean inhibitor indicating that it is a seninoproeinase |
|---|