The reduction of disulphides by human erythrocytes

Abstract

Cystamine and a number of cystamine derivatives are reduced at a rapid rate. The reduction most likely proceeds via spontaneous exchange reactions with intracellular glutathione, the oxidized glutathione formed being reduced by glutathione reductase. Tetrathionate, cystine ethyl ester and the disulphides of mercaptoethanol and of thioglycollic acid are reduced, but at a much slower rate than cystamine. Physiological disulphides (oxidized glutathione, cystine and homocystine) are not reduced at all, owing to an impermeability of the erythrocytes to these compounds. When human erythrocytes are stored in the conventional acid citrate[long dash]glucose buffer, a rapid decline in di sulphide-reducing capability is observed.