Abstract
Anticonvulsant drugs of the heterocyclic amide family inhibit in vitro enzymatic activity of Ca 2+ , Mg 2+ -ATPase of sarcoplasmic reticulum, the activated transmembrane calcium-ion transfer/ATP hydrolysis specific rate ratio being retained to provide lower concentrations of calcium ions in myofibrilla and relaxed muscles. Ethosuximide is a noncompetitive inhibitor with reversible action on basic enzyme catalyzed processes. The inhibition of the hydrolytic activity of the enzyme under the action of ethosuximide, phenytoin, and primidone was compared to their effect on other phosphatases (cAMP phosphodiesterase and Na + , K + -dependent ATPase).
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