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  • Title: [The importance of phosphatidylcholine in the binding of anti-D to human erythrocyte ghost membrane (author's transl)].
    Author: Kropp J, Weicker H.
    Journal: Z Immunitatsforsch Exp Klin Immunol; 1975 Sep; 150(3):267-76. PubMed ID: 127477.
    Abstract:
    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.
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