A red cell band 3 variant with altered stilbene disulphonate binding is associated with the Diego (Dia) blood group antigen

• Published in: Biochemical journal 1992-12, Vol.288 (3), p.713-716
• Main Authors: SPRING, F. A, BRUCE, L. J, ANSTEE, D. J, TANNER, M. J. A
• Format: Article
• Language: English
• Subjects: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid - analogs & derivatives; 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid - metabolism; Anion Exchange Protein 1, Erythrocyte - genetics; Anion Exchange Protein 1, Erythrocyte - immunology; Anion Exchange Protein 1, Erythrocyte - metabolism; Antigens; association; Band 3 protein; Biological and medical sciences; Blood group antigens; Blood Group Antigens - physiology; blood group Di super(a); erythrocytes; Erythrocytes - immunology; Erythrocytes - metabolism; Extracellular Space - metabolism; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Genetic Variation - physiology; Humans; isoforms; man; Molecular immunology; Polymorphism, Genetic; Protein Binding
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/bj2880713

1. We have shown that the Dia antigen of the Diego blood group system is associated with the presence of red cell band 3 Memphis, but not all band 3 Memphis samples carry the Dia antigen. 2. The band 3 Memphis associated with the Dia antigen was covalently labelled by 4,4'-di-isothiocyanato-1,2-diphenylethane-2,2'-disulphonic acid (H2DIDS) more readily than was normal band 3 or band 3 Memphis not associated with the Dia antigen. This altered reactivity with H2DIDS has previously been noted for a band 3 Memphis sub-type designated variant 2. 3. This is the first example of a band 3 polymorphism associated with an antigenic change in the extracellular region of the band 3 polypeptide and with altered H2DIDS binding.