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Toxicity of chlorpyrifos‐methyl to Sitophilus zeamais collected in Korea and biochemical differences
Authors:Won‐Sik Choi  Sung‐Eun Lee
Institution:1. Department of Life Science and Biotechnology, Soonchunhyang University, Asan, Korea;2. School of Applied Biosciences, Kyungpook National University, Daegu, Korea
Abstract:In this study, lethal concentration (LC50) values of chlorpyrifos‐methyl (CPM) were determined for two Korean strains (CBNU and KNU) of Sitophilus zeamais. The two strains had similar susceptibilities (1.70 and 1.86 μg a.i./cm2, respectively) to CPM. Carboxylesterase (CE) activity was twice as high in the CBNU strain as in the KNU strain. Lower acetylcholinesterase (AChE) activity was also noted in the latter; however, the activity of glutathione S‐transferase (GST) was twice as high as in the CBNU strain. Gel electrophoresis of CE of crude extracts from adults of the two strains of S. zeamais showed clearly different band patterns, with molecular weights of 60 kDa and 71 kDa in the CBNU and KNU strains, respectively. MALDI‐TOF MS/MS was used to profile small proteins (less than 10 kDa), with results indicating that 206 proteins are expressed differently in the two strains. The peak of interest of 2247.7 m/z was applied to TOF‐TOF MS and its de novo peptide sequence was identified as a tyrosine phosphatase fragment. Phospholipids from the two strains were analyzed and 34 phospholipids were found to be significantly different between strains. Results suggest that the two strains collected from Korea showed different biochemical results, presumably differences in insecticide selection by different living locations.
Keywords:chlorpyrifos‐methyl  de novo peptide sequence  glutathione S‐transferase  MALDI‐TOF MS/MS  Sitophilus zeamais
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