Article
Determinants of substrate specificity of a second non-neuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis.
European journal of biochemistry - 1 Apr 2000
Hussein A S, Smith A M, Chacón M R, Selkirk M E
Abstract excerpt
We recently reported on a non-neuronal secreted acetylcholinesterase (AChE B) from the nematode parasite Nippostrongylus brasiliensis. Here we describe the primary structure and enzymatic properties of a second secreted variant, termed AChE C after the designation of native AChE isoforms from this parasite. As for the former enzyme, AChE C is truncated at the carboxyl terminus in comparison with the Torpedo AChE,...
Topics
- Acetylcholinesterase
- Acetylthiocholine
- Amino Acid Sequence
- Animals
- Benzenaminium, 4,4'-(3-oxo-1,5-pentanediyl)bis(N,N-dimethyl-N-2-propenyl-), Dibromide
- Cholinesterase Inhibitors
- Cloning, Molecular
- Electrophoresis, Polyacrylamide Gel
- Isoenzymes
- Molecular Sequence Data
- Mutation
- Nippostrongylus