The Primary Sequence of Acetylcholinesterase and Selective Antibodies for the Detection of Organophosphate Toxicity
Abstract
Acetylcholinesterase polymorphism is a consequence of alternative MRNA processing which gives rise to two distinct molecular species of acetylcholinesterase. The work summarized in the progress report characterized the protein structure of acetylcholinesterase from Torpedo and correlated it with the organization of the gene. A divergence is found at the carboxyl terminus of the molecule giving rise to a hydrophilic, oligomeric and a glycophospholipid linked species. Antibodies which react uniquely with each form of the enzyme have been prepared which revealed each enzyme species to be localized at distinct positions with the synapse. Other antibodies defined a unique carbohydrate epitope on the glycophospholipid linked form and revealed that the active center of the enzyme is occluded from the surface. Distinct epitopes within the active center of the enzyme were also delineated. Lastly, we have developed an expression system using a Spodoptera- baculovirus system which has enabled us to express recombinant derived enzymes in large quantity.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 07, 1991
- Accession Number
- ADA246048
Entities
People
- Palmer W. Taylor
Organizations
- University of California, San Diego