Change of enzyme properties caused by cross-linking treatment of human erythrocytes.
Aragon et al [4] reported that rat erythrocytes can be cross-linked and permeabilized without significant inactivation or alterations of several enzymes in the glycolytic pathway. If this is the case, in situ kinetic analysis of the red cell enzymes in normal human red cells and abnormal red cells associated with hemolytic problems could be performed. However, we found that the treatment of human red cells with several bifunctional cross-linking reagents under various conditions always caused a certain extent of inactivation and a change in kinetic properties of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and lactate dehydrogenase. Thus, the cross-linking and permeabilization method, as it stands, is not satisfactory for in situ kinetic analysis of red cell enzymes.
D002463:Cell Membrane Permeability / Q000187:drug effects; D003432:Cross-Linking Reagents / Q000494:pharmacology*; D004120:Dimethyl Suberimidate / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism; D006801:Humans; D007096:Imidoesters / Q000494:pharmacology; D007700:Kinetics; D014051:Toluene 2,4-Diisocyanate / Q000494:pharmacology
D003432:Cross-Linking Reagents; D007096:Imidoesters; D014051:Toluene 2,4-Diisocyanate; D004120:Dimethyl Suberimidate; C007471:dimethyl dithiobispropionimidate; D005954:Glucosephosphate Dehydrogenase