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Clinical Chemistry 34: 518-524, 1988;
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Clinical Chemistry, Vol 34, 518-524, Copyright © 1988 by American Association for Clinical Chemistry

Quinidine-induced inhibition of leukocyte esterases

OT Markovic, DS Young and NS Markovic
Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia 19104-4283.

We have demonstrated the feasibility of a system based on image processing to measure enzyme activity inside morphologically classified individual cells. When used in this system, quinidine inhibited naphthol AS-D chloroacetate esterase in polymorphonuclear neutrophils and alpha-naphthyl acetate esterase and alpha-naphthyl butyrate esterase in monocytes. These effects were dependent on the duration of exposure and on drug concentration. Dose-effect relationships were established and the concentration at which 50% inhibition (ID-50) occurred was used as a reference point to compare the toxicity of different compounds. Chloroquine, primaquine, and quinine (which, like quinidine, possess a quinoline ring) also affected the esterases, but had no effect on several other enzymes. Neostigmine inhibited the esterases we studied but only at a very high concentration. Various chemicals inhibited the enzymes within the cells, as has been demonstrated for the enzymes in plasma.




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