Article
Anionic site interactions in human butyrylcholinesterase disrupted by two single point mutations.
The Journal of biological chemistry - 5 Dec 1990
Neville L F, Gnatt A, Padan R, Seidman S, Soreq H
Abstract excerpt
Structure-function relationships of recombinant human butyrylcholinesterase (CHE) variants were investigated by Xenopus oocyte microinjection. A Ser-425 to Pro-425 mutation failed to modify ligand binding properties. In contrast, Asp-70 to Gly-70 substitution significantly reduced CHE binding cap...
Topics
- Anions
- Binding Sites
- Brain Neoplasms
- Butyrylcholinesterase
- Cholinesterase Inhibitors
- DNA, Neoplasm
- Dibucaine
- Genetic Variation
- Glioma
- Humans
- Mutagenesis, Site-Directed
- Neuroblastoma
- Recombinant Proteins
- Substrate Specificity
- Succinylcholine