Structural comparison of glycophorins and immunochemical analysis of genetic variants
- 1 February 1978
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 271 (5645) , 519-524
- https://doi.org/10.1038/271519a0
Abstract
Differences in amino acid sequence of human erythrocyte membrane glycophorin A are correlated with M or N blood group activity. A 2nd sialoglycoprotein, glycophorin B, has an amino acid sequence identical to that of glycophorin AN in the first 23 positions and carries N activity only, suggesting that different structural genes code for the glycoproteins carrying these antigens. Certain genetically variant cells lack glycophorin A, as determined by immunochemical methods, and serological MN activity. Other variants lack MN activity, but contain normal amounts of glycophorin A in the membrane.Keywords
This publication has 37 references indexed in Scilit:
- Immunochemical evidence for the transmembrane orientation of glycophorin AJournal of Molecular Biology, 1977
- The amino acids of M and N blood group glycopeptides are differentBiochemical and Biophysical Research Communications, 1977
- STUDIES ON THE MEMBRANE GLYCOPROTEIN DEFECT OF En(a‐) ERYTHROCYTESInternational Journal of Immunogenetics, 1976
- Heterogeneity of the sialoglycoproteins of the normal human erythrocyte membraneBiochemical and Biophysical Research Communications, 1976
- Heterogeneity of human red cell membrane sialoglycoproteinsAnnals of Hematology, 1976
- Fractionation of the major sialoglycopeptides of the human red blood cell membraneBiochemical and Biophysical Research Communications, 1975
- IMMUNOCHEMICAL ASPECTS OF THE MNSs‐BLOOD GROUP SYSTEMInternational Journal of Immunogenetics, 1975
- Permanent Mixed‐Field Polyagglutinability (PMFP)Vox Sanguinis, 1973
- Anti‐N Reagents in Elucidation of the Genetical Basis of Human Blood‐Group MN Specificities1Vox Sanguinis, 1972
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970