diamide and Anemia--Hemolytic--Congenital

Proteins and phospholipids of platelets and red cell membranes of glucose-6-phosphate-dehydrogenase-deficient patients with chronic hemolytic disease were investigated. The enzyme deficiency is not connected with alteration in the protein and phospholipid pattern of platelets. However, marked differences in the diamide-induced protein polymerization between normal and deficient platelets were found. Whereas normal platelets show only a weak polymerization which is reversible during diamide incubation of the cells, the deficient platelets demonstrate a considerable and long lasting protein polymerization. The results point to a direct connection between the thiol-disulfide status of platelets and intracellular level of glutathione, which is able to repair oxidative damages. Two of the six patients showed already protein polymers in their erythrocyte membrane without addition of any SH-oxidizing agent. The phospholipid pattern of the deficient red-cell membranes were comparable to the controls.

Topics: Adolescent; Adult; Aged; Anemia, Hemolytic, Congenital; Blood Platelets; Blood Protein Electrophoresis; Blood Proteins; Child; Diamide; Erythrocyte Membrane; Glucosephosphate Dehydrogenase; Glucosephosphate Dehydrogenase Deficiency; Glutathione; Humans; Phospholipids