Catalytic and inhibitory properties of a major molecular form of acetylcholinesterase isolated from Lygus hesperus knight (Hemiptera: Miridae) |
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| Affiliation: | 1. Guangdong Engineering Research Center for Insect Behavior Regulation, College of Plant Protection, South China Agricultural University, Guangzhou, Guangdong 510642, China;2. School of Life Sciences, Arizona State University, Tempe, AZ 85281, USA;3. College of Art and Design, Hunan Applied Technology University, Changde, Hunan 415100, China;1. Key Laboratory of Biology, Genetics and Breeding of Special Economic Animals and Plants, Ministry of Agriculture and Rural Affairs, Tea Research Institute, Chinese Academy of Agricultural Science, Hangzhou 310008, People''s Republic of China;2. Key Laboratory of Forest Disaster Warning and Control of Yunnan Province, Southwest Forestry University, Kunming 650224, People''s Republic of China;3. East China Academy of Inventory and Planning of NFGA, Hangzhou 310008, People''s Republic of China;1. Laboratório de Química e Função de Proteínas e Peptídeos, Centro de Biociências e Biotecnologia, Universidade Estadual do Norte Fluminense Darcy Ribeiro - UENF, Campos dos Goytacazes, RJ 28013-602, Brazil;2. Laboratório de Melhoramento Genético Vegetal, Centro de Ciências e Tecnologias Agropecuárias, Universidade Estadual do Norte Fluminense Darcy Ribeiro - UENF, Campos dos Goytacazes, RJ 28013-602, Brazil;3. Laboratório de Biotecnologia, Centro de Biociências e Biotecnologia, Universidade Estadual do Norte Fluminense Darcy Ribeiro - UENF, Campos dos Goytacazes, RJ 28013-602, Brazil |
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| Abstract: | - 1.1. The major form of acetylcholinesterase (AChE) from Lygus hesperus demonstrated a greater affinity to selected substrates than unresolved AChE.
- 2.2. The turnover numbers of the native AChE were 7000 min−1 for acetylthiocoline, 4800 for acetyl-(β-methyl) thiocholine, 3000 for propionylthiocholine, and 390 for S-butyrylthiocholine.
- 3.3. Each molecule of the major form had two active sites and each subunit had one active site.
- 4.4. Paraoxon or dichlorvos had a higher affinity to the major AChE form than to the unresolved AChE, resulting in a higher potency for the inhibition.
- 5.5. Some references of comparison are also made with AChE from other animal species.
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