The Primary Sequence of Acetylcholinesterase and Selective Antibodies for the Detection of Organophosphate Toxicity
Abstract
Studies are directed to the chemical structure of acetylcholinesterase, with particular reference to the positions and identification of amino acid residues involved in catalysis, inhibitor binding, secretion and linkage to structural subunits. This work is dependent on the known primary structure of acetylcholinesterase and involves the use of site- directed covalent inhibitors of the active site and peripheral amionic site, selective antibodies and peptide isolation. The work has been developed to complement ongoing molecular biological studies of enzyme structure and site- specific mutagenesis. (To date, our studies have shown that the catalytic subunits from the asymmetric and glycophospholipid forms of the enzyme diverge at residue 534 in the C-terminus of the molecule. Epitopes to the antibodies 2C- 9 and 4E-7 have been tentatively assigned. Using these and other antibodies we have determined the localization of the asymmetric and glycophospholipid containing forms of the enzyme in the synapse.) (JES)
Document Details
- Document Type
- Technical Report
- Publication Date
- Nov 30, 1989
- Accession Number
- ADA225175
Entities
People
- Palmer W. Taylor
Organizations
- University of California, San Diego