Purification of a larval esterase from the Coatzacoalcos strain of Boophilus microplus Control de resistencia en garrapatas y moscas de importancia veterinaria y enfermedades que transmiten
Por: Pruett, J.H
| Miller, R.J | Jamroz, R.C | Guerrero, F.D | Industria Farmaceútica Veterinaria, México, D.F. (México) | Comisión Nacional de Sanidad Agropecuaria, México, D.F. (México) | Instituto Nacional de Investigaciones Forestales, Agrícolas y Pecuarias (INIFAP) México D.F., México | AMPAVE, México, D.F. (México) | FILASA, México, D.F. (México) | IICA, México, D.F. (México) | 4. Seminario Internacional de Parasitología Animal Puerto Vallarta, Jalisco (México) 20-22 Oct 1999.
Tipo de material: 
ArtículoEditor: Puerto Vallarta, Jalisco (México) 1999Descripción: p. 67-68.Tema(s): MEXICO | BOOPHILUS MICROPLUS | ESTERASAS | MEXICO AGRICULTURA | BOOPHILUS MICROPLUS AGRICULTURA | ESTERASES AGRICULTURA | MEXIQUE AGRICULTURA | BOOPHILUS MICROPLUS AGRICULTURA | ESTERASE AGRICULTURAResumen: The objectives of this ongoing work are to purify and investigate a Cz strain metabolic esterase designated as EST9. We note intense hydrolytic activity in the region of this protein band (R 0,6,8 percent gel) on polycrylamide gels (PAGE), Hydrolysis of the general esterease substrate, naphthyl acetate, and the pyrethroid acaricide permtethrin, by extracted proteins was 4,5 fold greater for the Cz strain than for an acaricide suscpetible control stain. The enhanced activity and/or overexpression of EST9 esterase suggests a possible mechanistic role for this esterase in the observed resistance to pyrethroid and organophosphate acaricides
| Tipo de ítem | Ubicación actual | Colección | Signatura | Estado | Fecha de vencimiento | Código de barras |
|---|---|---|---|---|---|---|
Analítica
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Sede Central | Colección IICA | IICA-L73 11 (Navegar estantería) | Disponible | BVE2765111085 |
Navegando Sede Central Estantes , Código de colección: Colección IICA Cerrar el navegador de estanterías
The objectives of this ongoing work are to purify and investigate a Cz strain metabolic esterase designated as EST9. We note intense hydrolytic activity in the region of this protein band (R 0,6,8 percent gel) on polycrylamide gels (PAGE), Hydrolysis of the general esterease substrate, naphthyl acetate, and the pyrethroid acaricide permtethrin, by extracted proteins was 4,5 fold greater for the Cz strain than for an acaricide suscpetible control stain. The enhanced activity and/or overexpression of EST9 esterase suggests a possible mechanistic role for this esterase in the observed resistance to pyrethroid and organophosphate acaricides
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