Erythrocyte glutathione reductase deficiency is seen in deficiency of:

Ans: A (Riboflavin) Ref: Glatzle D, Korner HF Christeiier S. Wiss O. Method for the detection of a biochemical riboflavin deficiency. Stimulation of NADBH2-dependent glutathione reductase from human erythrocytes by FAD in vitro. Investigations on the vitamin B2 status in healthy people and geriatric patients. Int. J Vitam Res 1970:40:166-183Explanation:Glutathione, in reduced form (GSH), maintains cell membrane integrity against oxidative stress by acting as a substrate for the reduction of peroxides to less damaging alcohols by glutathione peroxidase.Glutathione reductase facilitates this process by catalysing the conversion of oxidized glutathione (GSSG) to GSH, thereby maintaining an adequate level of intracellular GSH.Optimal glutathione reductase activity depends on adequate availability of flavin adenine dinucleotide (FAD), a coenzyme derived from riboflavin (vitamin B-2).Thus glutathione reductase activity is suboptimal in individuals with riboflavin deficiency.Riboflavin (vitamin B-2) is a water soluble B vitamin that serves as a precursor of FAD and flav in mononucleotide.These two compounds are important coenzymes in a variety of electron transfer reactions during energy producing, biosynthetic, detoxifying and electron scavenging processes.