Article
Active site mutant acetylcholinesterase interactions with 2-PAM, HI-6, and DDVP.
Biochemical and biophysical research communications - 14 Apr 2006
Kovarik Zrinka, Ciban Nikolina, Radić Zoran, Simeon-Rudolf Vera, Taylor Palmer
Abstract excerpt
We used mouse recombinant wild-type acetylcholinesterase (AChE; EC 3.1.1.7), butyrylcholinesterase (BChE; EC 3.1.1.8), and AChE mutants with mutations (Y337A, F295L, F297I, Y72N, Y124Q, and W286A) that resemble residues found at structurally equivalent positions in BChE, to find the basis for divergence between AChE and BChE in following reactions: reversible inhibition by two oximes, progressive inhibition by...
Topics
- Acetylcholinesterase
- Animals
- Binding Sites
- Dichlorvos
- Drug Interactions
- Mice
- Mutation
- Oximes
- Pralidoxime Compounds
- Pyridinium Compounds
- Recombinant Proteins
