A new natural anti-alpha-galactosyl IgG antibody (anti-Gal) was found to be present in high titer in the serum of every normal individual studied. The antibody was isolated by affinity chromatography on a melibiose-Sepharose column. The reactivity of the antibody was assessed by its interaction with alpha-galactosyl residues on rabbit erythrocytes (RabRBC). The specificity was determined by inhibition experiments with various carbohydrates. The anti-Gal interacts with alpha-galactosyl residues, possibly on glycolipids of human RBC (HuRBC), after removal of membrane proteins by treatment with pronase. In addition, the anti-Gal bind specifically to normal and pathologically senescent HuRBC, suggesting a physiological role for this natural antibody in the aging of RBC. The ubiquitous presence of anti-Gal in high titers throughout life implies a constant antigenic stimulation. In addition to the theoretical interest in the antibody, the study of the anti-Gal reactivity seems to bear immunodiagnostic significance. Decrease in the antibody titer was found to reflect humoral immunodeficiency disorders.
Article| November 01 1984
A unique natural human IgG antibody with anti-alpha-galactosyl specificity.
E A Rachmilewitz,
E A Rachmilewitz
Online ISSN: 1540-9538
Print ISSN: 0022-1007
J Exp Med (1984) 160 (5): 1519–1531.
U Galili, E A Rachmilewitz, A Peleg, I Flechner; A unique natural human IgG antibody with anti-alpha-galactosyl specificity.. J Exp Med 1 November 1984; 160 (5): 1519–1531. doi: https://doi.org/10.1084/jem.160.5.1519
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