Substrate specificities and multiple forms of esterases in the brown planthopper, Nilaparvata lugens (Stal)

• Published in: Pesticide biochemistry and physiology Vol. 27; no. 1; pp. 30 - 35
• Main Authors: Chang, C.K., Whalon, M.E.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 1987; Elsevier
• Subjects: Applied sciences; Biological and medical sciences; Chemical control; Control; Delphacidae; esterasas; esterase; esterases; Exact sciences and technology; Fundamental and applied biological sciences. Psychology; Generalities; growing media; indonesia; indonesie; medio de cultivo; nilaparvata; Nilaparvata lugens; oryza sativa; Other techniques and industries; pesticide resistance; Phytopathology. Animal pests. Plant and forest protection; Protozoa. Invertebrates; resistance aux pesticides; resistencia a los plaguicidas; substrat de culture; toxicologia; toxicologie; toxicology; Heteroptera; Pest; Insecticide; Esterase; Enzyme; Arthropoda; Insecta; Chemical control; Nilaparvata lugens; Delphacidae; Invertebrata; Negative therapeutic reaction
• ISSN: 0048-3575; 1095-9939
• DOI: 10.1016/0048-3575(87)90092-7

Substrate specificities have been examined in body homogenates of the brown planthopper, Nilaparvata lugens (Stal), using α-naphthyl acetate, β-naphthyl acetate, trans-permethrin, cis-permethrin, malathion, and fenvalerate as substrates. Eight esterases were resolved from body homogenates of the brown planthopper with p I values in the range of 4.3–5.3 and designated as E1–E8. All E1–E8 hydrolyzed α-naphthyl acetate, β-naphthyl acetate, cis-permethrin, trans-permethrin, and malathion at different rates. Fenvalerate was the most stable substrate to hydrolysis and was hydrolyzed by E1–E8 except E3.