Abstract
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.
MeSH Terms
Adult
Aged
Aging
Animals
Antibody Specificity
Binding Sites, Antibody
Blood Donors
Child
Child, Preschool
Chromatography, Affinity
Erythrocytes/metabolism,ultrastructure
Galactose/immunology
Humans
Immunoglobulin G/immunology,isolation & purification,physiology
Immunologic Deficiency Syndromes/immunology
Infant
Infant, Newborn
Rabbits
Chemicals
Immunoglobulin G
Galactose
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Galili U
Rachmilewitz E A
Peleg A
Flechner I
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