Chemical modification of acetylcholinesterase with methoxypolyethylene glycol |
| |
Authors: | Delphine Garcia Jean-Louis Marty |
| |
Institution: | 1. Centre de Phytopharmacie, URA CNRS 461, Université de Perpignan, 52 avenue de Villeneuve, 66860, Perpignan Cedex, France
|
| |
Abstract: | Acetylcholinesterase (AChE) (EC 3.1.1.7) was modified with activated monomethoxypolyethylene glycol (mPEG). A decrease of 50% in the catalytic activity was measured during the coupling reaction and the change in the surface properties of AChE was used to separate by hydrophobic interaction chromatography the native and the modified enzyme. The native and the modified enzymes were found to have the same optimalcatalytic conditions. Moreover, the Michaelis constant of both enzymes were similar, whereas theV m and the bimolecular-velocity constant calculated for organophosphorus inhibitors were slightly higher for the modified AChE. Finally, the modification with mPEG did not improve the thermal stability, whereas the stability in a few organic solvents increased. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|