SYNTHESIS AND SOME REACTIONS OF PANTETHEINE-GLUTATHIONE MIXED DISULFIDE

The mixed disulfide of pantetheine and glutathione was synthesized by thiolysis with glutathione of the thiolsulfonate analogue of pantethine. The product was purified by ion-exchange chromatography and was obtained in a chromatographically and electrophoretically homogeneous form. Positive reactions were obtained by development with ninhydrin, fluorescein mercuric acetate, and sodium borohydridenitroprusside. The quantitative analyses for pantetheine and disulfide content were consistent with the expected structure. The mixed disulfide of pantetheine and glutathione was a poor substrate for glutathione reductase, and caused a time-dependent inactivation of the enzyme, which was increased in the presence of NADPH. The substance was also an inhibitor of S-lactylglutathione lyase (glyoxalase I"). It did not inhibit 3-hydroxyacyl-CoA dehydrogenase. The latter enzyme was assayed with S-acetoacetyl-N-acetylcysteamine and NADH as substrates (Km values are reported). © 1969."