The influence of thiol groups in the activity of dehydrogenases. II

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Abstract
While the succinic dehydrogenase was inactivated by incubation with GSSG and its activity restored by subsequent incubation with GSH this treatment had no effect on the other dehydrogenases studied. Alloxan in low concs., as an oxidant of SH-groups, inactivated the succinic enzyme but not the other dehydrogenases. The succinic enzyme was inactivated by Cu and by maleic and iodoacetic acids, substances which reacted with SH groups. They had little or no effect on the other enzymes tested. Malonic, succinic and fumaric acids protected the succinic dehydrogenase from the influence of GSSG. The exptl. results indicated that the succinic dehydrogenase required for its activity the integrity of SH groups in its structure while this was not the case with other typical dehydrogenases. When muscle tissue was exhaustively extracted with salt solns. dehydrogenases remained active in the residual structure of the fibres, which still showed cross striation and birefringence.

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