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Anti‐Di b as a red cell autoantibody
Author(s) -
Issitt P.D.,
Combs M.R.,
Allen J.,
MelroyCarawan H.
Publication year - 1996
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1046/j.1537-2995.1996.36996420757.x
Subject(s) - autoantibody , epitope , red cell , band 3 , antibody , anion exchanger , red blood cell , b cell , microbiology and biotechnology , immunology , biology , chemistry , biochemistry , medicine , ion exchange , erythrocyte membrane , ion , organic chemistry , membrane
Background: It is known that some “warm”‐reactive autoantibodies are directed against epitopes on the red cell anion exchanger, protein band 3. Some such antibodies (but not all) recognize Wr b . It is also known that Di a and Di b represent an amino acid polymorphism of band 3. Study Design and Methods: Autoantibodies from 119 patients were tested against Di(b‐) red cells. Seventy‐four of these autoantibodies were subsequently absorbed with Di(b‐) red cells. Results: All 119 autoantibodies initially reacted with the Di(b‐) red cells, which showed that none contained only anti‐Di b . Among the 74 adsorbed with Di(b‐) red cells, two were found to contain an unadsorbed anti‐Di b component. Conclusion: No example of autoanti‐Di b as the only autoantibody present was found among the 119 samples tested. However, 2 (2.7%) of 74 autoantibodies subjected to adsorption with Di(b‐) red cells were seen to contain an anti‐Di b component. This low incidence of autoanti‐Di b is in marked contrast to the high incidence of autoanti‐Wr b , although both antibodies define epitopes associated with the red cell anion exchanger, band 3.