Über den Einfluß von Snlfhydrylverbindungen auf enzymatische Prozesse.

Abstract

In previous publications it was shown that the cooperation of the sulfhydryl compounds is necessary for the function of the intracellularly effective proteinases. Glutathione was identified as the natural activator. The results of B. H. Kleinmann can be explained by the fact that the enzyme solutions were previously activated. Cathepsin Without its natural activator was not effective with any protein studied. The sulfhydryl compounds also influenced other enzyme processes. Arginase was activated by SH compounds in the presence of heavy metals (Fe or Cu). Other enzymes were inhibited by SH, for example, the hydrolysis of phosphoric ester by phosphatase, while the synthesis was not influenced. Since iodoacetic acid is oxidized by SH, the strong hydrolysis of creatine phosphoric acid by iodoacetic acid-poisoned muscle is explained. Catalase was inhibited by SH. The inhibition in this case was in part irreversible. Iron (in catalase Fe[image]) was reduced by sulfhydryl. The possibility that the anticatalase in blood described by Batelli and Stern is identical with sulfhydryl compounds is discussed.