PURIFICATION AND PARTIAL CHARACTERIZATION OF A GLYCOPROTEIN WITH AMIDOLYTIC ACTIVITY OBTAINED FROM SNAKE VENOM BOTHROPS BARNETTI

Descripción del Articulo

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...

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Detalles Bibliográficos
Autores: Inga A., R., Lazo M., F., Yarlequé Ch., A., Vivas R., D.
Formato: artículo
Fecha de Publicación:2010
Institución:Universidad Nacional Mayor de San Marcos
Repositorio:Revistas - Universidad Nacional Mayor de San Marcos
Lenguaje:español
OAI Identifier:oai:ojs.csi.unmsm:article/4600
Enlace del recurso:https://revistasinvestigacion.unmsm.edu.pe/index.php/quim/article/view/4600
Nivel de acceso:acceso abierto
Materia:Venom
snake
amidolytic activity
glycoprotein
Bothrops barnetti
Veneno
serpiente
actividad amidolítica
glicoproteína
Descripción
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
PURIFICATION AND PARTIAL CHARACTERIZATION OF A GLYCOPROTEIN WITH AMIDOLYTIC ACTIVITY OBTAINED FROM SNAKE VENOM BOTHROPS BARNETTI
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