| Autor: |
B.A Khaskin, A.E. Khovanskikh, Abduvakhabov Aa, Tatyana A. Mastryukova, E.B. Maizel, Godovikov Nn, A.P. Brestkin, I.N. Sazonova, A. E. Shipov, K.V. Novozhilov, S.N. Moralev, M. I. Kabachnik |
| Rok vydání: |
1986 |
| Předmět: |
|
| Zdroj: |
Insect Biochemistry. 16:701-707 |
| ISSN: |
0020-1790 |
| DOI: |
10.1016/0020-1790(86)90014-4 |
| Popis: |
Anticholinesterase potency and toxicity for spring grain aphids of 52 organophosphorous inhibitors (OPI) of different structures were investigated. As regards sensitivity to OPI, the acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) of the spring grain aphid are shown to differ significantly from the “typical” cholinesterases, i.e. from human erythrocyte AChE and horse serum BuChE, which is presumably associated with differences in the structures of the active surface of these enzymes. The extremely high sensitivity of spring grain aphid AChE to cationic OPI containing the onium atom in the leaving part of the molecule indicates the fundamental importance of the anionic site in the active centre of the enzyme. By contrast, spring grain aphid BuChE has low sensitivity to OPI, typical of the cationic type, which suggests that it has no anionic site. Correlation was established between the toxicity and anticholinesterase potency of OPI which contain no cationic groups or bulky hydrophobic radicals. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
