Studies of lactate dehydrogenase in the purified state and in intact erythrocytes.
Lactate dehydrogenase in intact erythrocytes was studied by observing isotope exchange between lactate and pyruvate by p.m.r. The inhibition of the enzyme in intact cells by both oxalate and pyruvate was found to be similar to that of the purified enzyme. The activity of the enzyme in intact cells indicates that the free solution NAD+ + NADH concentration in erythrocytes is about 10 microM whereas the total extractable NAD+ + NADH is about 80 nmol/ml of cell water.
D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors / Q000097:blood*; D007773:Lactates / Q000378:metabolism; D019344:Lactic Acid; D009682:Magnetic Resonance Spectroscopy; D008954:Models, Biological; D009243:NAD / Q000378:metabolism; D010070:Oxalates / Q000494:pharmacology; D019815:Oxalic Acid; D011773:Pyruvates / Q000494:pharmacology; D019289:Pyruvic Acid
D007773:Lactates; D010070:Oxalates; D011773:Pyruvates; D009243:NAD; D019344:Lactic Acid; D019289:Pyruvic Acid; D019815:Oxalic Acid; D007770:L-Lactate Dehydrogenase