Hydrolysis of organophosphorus compounds by an esterase isozyme from insecticide resistant pest Helicoverpa armigera.
Esterase activity of resistant and susceptible H. armigera were compared in gels with different substrate such as naphthyl acetate, naphthyl phosphate, paraoxon and monocrotophos. Whole body extract of resistant H. armigera hydrolyzed paraoxon, monocrotophos and naphthyl phosphate in gels. Resistant H. armigera showed high esterase, phosphatase and paraoxon hydrolase activity compared to susceptible ones.
Srinivas
R
R
Department of Biochemistry, Gulbarga University, Gulbarga 585 106, India.
Jayalakshmi
S K
SK
Sreeramulu
K
K
D000818:Animals; D004950:Esterases / Q000378:metabolism*; D006868:Hydrolysis; D007305:Insecticide Resistance; D007306:Insecticides / Q000378:metabolism*; D007814:Larva / Q000187:drug effects / Q000254:growth & development / Q000378:metabolism; D007915:Lepidoptera / Q000378:metabolism*; D008999:Monocrotophos / Q000378:metabolism; D009281:Naphthalenes / Q000378:metabolism; D009284:Naphthols / Q000378:metabolism; D009943:Organophosphorus Compounds / Q000378:metabolism; D010261:Paraoxon / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism
D007306:Insecticides; D009281:Naphthalenes; D009284:Naphthols; D009943:Organophosphorus Compounds; C005366:naphthyl acetate; C014694:naphthyl phosphate; D008999:Monocrotophos; D004950:Esterases; D010744:Phosphoric Monoester Hydrolases; D010261:Paraoxon