Abstract
Summary
When erythrocytes are treated with glutaraldehyde they become resistant to hemolytic agents (water) and to mechanical stresses (sonication, freeze-thawing). These alterations are accompanied by the irreversible inactivation of acetylcholinesterase, an integral part of the erythrocyte membrane. Enzyme inactivation is dependent on concentration, pH, time and temperature. The reduction in activity is not associated with changes in substrate specificity, Km and pH profile. However, the residual acetylcholinesterase activity is more labile to denaturation by heat and urea than the normal enzyme.
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