Carboxylesterases from Boophilus microplus hydrolyze trans-permethrin |
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| Authors: | Peter W Riddles Patricia A Davey James Nolan |
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| Institution: | CSIRO, Division of Tropical Animal Science, Long Pocket Laboratories, Private Bag No. 3, Indooroopilly, Queensland 4068, Australia |
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| Abstract: | An esterase which hydrolyzes the ester bond of trans-permethrin has been partially purified from homogenates of larvae of the cattle tick. The final (gel filtration) step showed two distinct peaks of p-nitrophenylbutyrate-hydrolyzing activity. The trans-permethrin-hydrolyzing activity of the lower-molecular-weight enzyme cochromatographed with the p-nitrophenylbutyrate-hydrolyzing activity of that enzyme. Little trans-permethrin hydrolysis was observed in the high-molecular-weight peak. The yield of the low-molecular-weight enzyme increased on extraction of the homogenates with Triton X-100. Inhibition studies using the low-molecular-weight enzyme and trans-permethrin as substrate indicated that hydrolysis was due largely to a carboxylesterase (EC 3.1.1.1). |
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| Keywords: | Present address: Department of Biochemistry Stanford University School of Medicine Stanford University Medical Center Stanford Calif 94305 To whom correspondence should be addressed |
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