ALPHA-METHYLDOPA AND THE ERYTHROCYTE-MEMBRANE

  • 1 January 1980
    • journal article
    • research article
    • Vol. 40  (3) , 554-560
Abstract
.alpha.-Methyldopa binds to human erythrocye membrane proteins. A portion of this binding is readily dissociable in SDS [sodium dodecyl sulfate], but a significant amount is very tightly bound and does not come off even under rigorous conditions. The binding is increased under oxidizing conditions and very much inhibited in the presence of reducing agents and superoxide dismutase and catalase. Hb competes with membrane peptides for .alpha.-methyldopa binding. Hb may act as a sink for the drug in the intact cell. The 1st step in the pathogenesis of Coombs positivity and hemolytic anemia may result from an alteration of a critical membrane peptide secondary to binding of the drug during normal membrane breakdown.