Acquired enzymopathy of erythrocyte glucose-6-phosphate dehydrogenase in acute viral hepatitis.
Erythrocyte glucose-6-phosphate dehydrogenase from patients with acute viral hepatitis has been purified and characterized. The enzyme showed decreased activity (relative to protein), reduced affinity for glucose 6-phosphate and was inactivated at 45 degrees C or at low pH values. The activity and properties of normal erythrocyte enzyme, incubated in vitro with blood plasma of patients, showed a similar pattern of modifications. Incubation with bilirubin affected the enzyme stability, but not its activity or affinity for substrate.
D001663:Bilirubin; D004912:Erythrocytes / Q000201:enzymology*; D005952:Glucose-6-Phosphatase / Q000378:metabolism; D005954:Glucosephosphate Dehydrogenase / Q000097:blood*; D006525:Hepatitis, Viral, Human / Q000097:blood / Q000201:enzymology*; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D009249:NADP / Q000378:metabolism
D009249:NADP; D005954:Glucosephosphate Dehydrogenase; D005952:Glucose-6-Phosphatase; D001663:Bilirubin