Maleic acid as inhibitor of enzyme reactions induced by SH-compounds

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Abstract
Maleic acid reacted with M/200 glutathione. The reaction could be detected in a physiological medium such as pig or ox liver but was not complete. Maleic acid reacted with proteins containing SH-groups. The activation of glyoxalase and of the anaerobic glucose breakdown by glutathione was decreased by maleic acid. The activities of succinodehydrogenase and of papain were decreased by maleic acid. The inhibition of the enzyme reactions investigated was connected with the interaction of maleic acid with thiol groups. The reactions of maleic acid in its application to enzyme reactions were discussed.