Abstract
The glyoxalase method for the estimation of glutathione has been adapted for use in the pH-stat. A new method for the estimation of glutathione based on thiol-di-sulphide exchange reactions with cystamine and glutathione reductase has been developed. The reactions are followed spectrophotometrically at 340 m[mu]. The method as described can estimate down to 0.1 /[mu]mole of glutathione. It has been compared with the glyoxalase method and found to give similar results with rat liver, brain and muscle. The averages of these were 7.32, 1-90 and 1.1 [mu]moles/g. fresh wt. respectively. Extracts of kidney tissue at pH 8.2, extracts of flour, and nicotinamide coenzymes form complexes with oxidized glutathione in such a way that it is unavailable for reduction by glutathione reductase.