[The importance of phosphatidylcholine in the binding of anti-D to human erythrocyte ghost membrane (author's transl)].
Incubation of Rh positive ghosts with phospholipase A2 and C abolished the adsorption of Rh antibodies on the ghosts; incubation with phospholipase D, however, did not affect their adsorption and none of these phospholipases affected the adsorption of antibodies of the ABO system. The impairment of antigen-antibody-reaction in Rh positive ghosts treated with phospholipase corresponds to the absence of the antigen-antibody reaction with the membrane protein associated with Rh characteristics in the Schultz-Dale-Test. The chromatogram of the phospholipids extracted from those stromata treated with various phospholipases and those not treated showed different patterns. After incubation with phospholipase-A2 the lecithin and cephalin streaks were reduced and in addition lysophosphatide and fatty acid streaks were detected. In the case of phospholipase C the lecithin and cephalin streaks were further reduced while diglyceride streaks made their appearance. The phospholipid extracts from those stromata treated with phospholipase D and those not treated were identical. Phospholipase C reduced the values of lipid phosphorus more than did phospholipase A2, while phospholipase D did not reduce them at all. This study supports the results of other investigators who have postulated that the Rh antigens are located in a lipoprotein on the membrane of the human erythrocyte. The antigen-antibody-reaction seems to require a precise protein-phospholipid interaction.
D001666:Binding Sites, Antibody; D002462:Cell Membrane / Q000276:immunology*; D004912:Erythrocytes / Q000276:immunology*; D006801:Humans; D007106:Immune Sera; D010206:Papain; D010713:Phosphatidylcholines; D010740:Phospholipases / Q000378:metabolism; D012204:Rh-Hr Blood-Group System
D007106:Immune Sera; D010713:Phosphatidylcholines; D012204:Rh-Hr Blood-Group System; D010740:Phospholipases; D010206:Papain
Die Bedeutung von Phosphatidylcholin für die Bindung von Anti-D an die Erythrozytenmembran