Question

explain how rbc's make NADH and NADPH and why they are necessary.

Answer 1

Glucose SLC2A1 Oxidative Stress Regulatory Pathway (Erythrocyte) Methylene Blue Pathway PD NADPH NADPH G-Phospho 6-Phospho gluconolactone Ribulose-5- phosphate NADP NADP (PGD G6PD PGLS HK1 Ribose-5- phosphate Glucose-6- phosphate 6-Phospho gluconate Glucose GPI PRPP Erythrocyte Adenine) Fructose-6- phosphate ADP ---- Glycolysis © PharmGKB

Pentose Phosphate pathway Glucose-6-p Oxidative phase NADP Glucose-6-phosphate dehydrogenase NADPH 6-Phosphogluconolactone Gluconolactonase 6-Phosphogluconate NADP 6-phosphogluconate dehydrogenase NADPH V CO, Ribulose-5-phosphate Non-oxidative phase Ribulose-5-phosphate Isomerase Ribulose-5-phosphate 3-Fein erase Ribose-5-phosphate Xylulose-5-phosphate Trans ketalase Glyceraldehyde 3-phosphate + Sedohep tulose 7-phosphate Transaldotare Fructose 6-phosphate + Erythrose 4-phosphate Xylulose-5-phosphate Trans het alase Glycolysis Glyceraldehyde 3-phosphate + Fructose 6-phosphate Glycolysis Glycolysis

One of the uses of NADPH in the cell is to prevent oxidative stress.

The major role of NADPH in red cells is to reduce the disulfide form of glutathione to the sulfhydryl form. The enzyme that catalyzes the regeneration of reduced glutathione, the flavoprotein glutathione reductase, a dimer of 50-kd subunits, is homologous to ferredoxin-NADP+ reductase, which we encountered in photosynthesis (Section 19.3.4). The reduced form of glutathione serves as a sulfhydryl buffer that maintains the cysteine residues of hemoglobin and other red-blood-cell proteins in the reduced state. Normally, the ratio of the reduced to oxidized forms of glutathione in red blood cells is 500.