Substrate specificities and multiple forms of esterases in the brown planthopper, Nilaparvata lugens (Stal)
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 bro...
Saved in:
Published in | Pesticide biochemistry and physiology Vol. 27; no. 1; pp. 30 - 35 |
---|---|
Main Authors | , |
Format | Journal Article |
Language | English |
Published |
San Diego, CA
Elsevier Inc
1987
Elsevier |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | 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. |
---|---|
Bibliography: | H H10 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 |
ISSN: | 0048-3575 1095-9939 |
DOI: | 10.1016/0048-3575(87)90092-7 |