Abstract
In order to characterize the fatty acid (FA)-induced inhibition of pseudocholinesterase (pchE), the interaction of pchE with FA (n-capric acid and n-lauric acid) and/or human serum albumin (HSA) was studied by electrophoreses on a cellulose acetate membrane and a polyacrylamide gel thin-layer. It was demonstrated that pchE binds with n-[1-14C] lauric acid, suggesting that the FA-induced inhibition of pchE activity is based on the interaction of the enzyme with FA. The binding of pchE with n-[1-14C] lauric acid was depressed by HSA. Consequently, the present results suggest that the reduction of FA-induced inhibition of pchE activity by HSA is associated closely with the depression of pchE-FA binding by HSA. Moreover, no selectivity in the n-capric acid-induced inhibition of pchE isozymes was found in the present study, i. e., all isozymes (C1-C4) of pchE were equally inhibited by n-capric acid.
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