Some properties of acetylcholinesterase partially purified from susceptible and resistant green rice leafhoppers, Nephotettix cincticeps Uhler (Hemiptera : Deltocephalidae)

• HAMA H.

  National Institute of Agricultural Sciences

• IWATA Toshikazu

  National Institute of Agricultural Sciences

• MIYATA Tadashi

  Laboratory of Applied Entomology and Nematology, Faculty of Agriculture, Nagoya University

• SAITO Tetsuo

  Laboratory of Applied Entomology and Nematology, Faculty of Agriculture, Nagoya University

抄録

Properties of acetylcholinesterases (AChE) in the green rice leafhopper were examined using partially purified normal and modified AChEs. The modified enzyme was much less sensitive to inhibitive by propoxur and malaoxon than the normal one, but highly sensitive to inhibition by diazoxon. Substrate specificity and effect of pH on activity of the normal enzyme were similar to those of the bovine erythrocyte AChE used as a reference enzyme, but those of the modified AChE were obviously different from those of the other enzymes. On the other hand, difference of the normal and modified AChEs in the Km values of substrates was rather small, i.e., by a factor of less than 2. It may be concluded that the modified AChE alters in a binding site, which is related to the reaction with inhibitors, but different from the site for the intrinsic substrate acethlcholine.

収録刊行物

• Appl. Entomol. Zool.

  Appl. Entomol. Zool. 15 249-261, 1980

  日本応用動物昆虫学会

詳細情報

• CRID: 1570854176912633472
• NII論文ID: 110001104865
• NII書誌ID: AA00543238
• ISSN: 00036862
• 本文言語コード: en
• データソース種別:
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