Ultrasensitive Detection of Chemical Substances
Quarterly rept. 1 Mar-31 May 1985
NEW MEXICO UNIV ALBUQUERQUE SCHOOL OF MEDICINE
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During the past quarter, we have produced and cloned several hybridomas with antibody against AChE or AChE-DFP conjugate. One of these antibodies, designed V16-6B, has special interest. As expected this antibody binds the AChE-DFP conjugate effectively and shows a lowered cross reaction with AChE alone. The remarkable feature of the antibody is that it does not appear to bind DFP significantly. Figure 1 shows the protective effect V16-6B has in inhibiting the inactivation of AChE by decreasing amounts of DFP. Normally, DFP will activate AChE rapidly, However, if an agent such as an antibody is introduced which binds DFP then the reaction between AChE and DFP will be slowed. This data is very preliminary and requires a number of further control experiments. These will include more accurate quantization of the antibody so that molar ratios and equilibrium binding conditions can be better established and control conditions include a protein such as non-reactive Goat IgG. This data does suggest, however, that V16-6B may be directed against an AChE site which changes determinant form of conformation when DFP binding takes place and that this site is probably not located at the active site of AChE. That AChE should have been a determinant site that changes its conformation when irreversibly bound to DFP is not surprising. This data is very interesting and suggest possibilities of detecting a wide variety of potential toxins that inactivate AChE.