Title : Biochemical Characterization of the Esterases Al and Bl Associated with Organophosphate Resistance in the Culex pipiens L. - Fournier_1987_Pestic.Biochem.Physiol_27_211 |
Author(s) : Fournier D , Bride JM , Mouches C , Raymond M , Magnin M , Berge JB , Pasteur N , Georghiou GP |
Ref : Pestic Biochem Physiol , 27 :211 , 2015 |
Abstract :
Two esterases, A1 and B1, displaying a high activity in organophosphate (OP) resistant Culex pipiens L. from southern France and in C. quinquefasciatus Say from California, respectively, have been analyzed. Both enzymes are shown to be soluble and to constitute a large proportion of the proteins (1-3% for esterase A1 and 6-12% for esterase B1). The size of native esterase A1 was estimated between 118 and 134 kDa, that of esterase B1 67 kDa. Upon SDS denaturation, esterase B1 leads a single polypeptide of 67 kDa which suggests that it is a monomeric protein; esterase A1 leads also a single polypeptide of 60 kDa suggesting a homodimeric structure of the protein. These observations are discussed with regards to esterase E4 of Myzus persicae Sultz. |
PubMedSearch : Fournier_1987_Pestic.Biochem.Physiol_27_211 |
PubMedID: |
Fournier D, Bride JM, Mouches C, Raymond M, Magnin M, Berge JB, Pasteur N, Georghiou GP (2015)
Biochemical Characterization of the Esterases Al and Bl Associated with Organophosphate Resistance in the Culex pipiens L.
Pestic Biochem Physiol
27 :211
Fournier D, Bride JM, Mouches C, Raymond M, Magnin M, Berge JB, Pasteur N, Georghiou GP (2015)
Pestic Biochem Physiol
27 :211