Structural Polymorphism of Glycophorins Demonstrated

We have explored the polymorphism of the glycophorin system in the human erythrocyte membrane using the immunoblotting techniques and examining 52 individuals selected without prior bias as to their serologic state and ten documented serologic variants of M, N, S. s blood group system. Polyclonal antisera to a glycophorin and to a glycophorin CNBr carboxyl terminal fragment C (residues 82-1 31 ) and M and N specific monoclonal antibodies (MoAbs) were used. The first two reagents detect specific regions of the a glycophorin molecule and all electrophoretically resolved species of glycophorins immunologically related to a and #{244} glycophorins (#{244} glycophorin. [a-#{246}] hybrids and other glycophorins with an alteration in the carboxyl terminal segment); the M and N MoAbs identified the glycophorin species containing or lacking the M or N