Self-association of human erythrocyte glycophorin A. Appearance of low mobility bands on sodium dodecyl sulfate gels.
We have examined the self-association of glycophorin A, the major sialoglycoprotein of the human erythrocyte membrane, using sodium dodecyl sulfate (SDS) polyacrylamide gels and circular dichroism. Pure glycophorin A has a tendency to form multiple bands on SDS gels at positions of higher apparent molecular weight than the PAS 1 and PAS 2 bands previously seen. These high molecular weight bands do not have mobilities corresponding to integral polymers of PAS 1 and PAS 2. Circular dichroism spectra of solutions giving rise to these bands or to PAS 1 and PAS 2 bands alone, indicate that these species all have essentially the same peptide conformation.
D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000378:metabolism*; D006021:Glycophorins / Q000097:blood*; D006801:Humans; D046911:Macromolecular Substances; D008970:Molecular Weight; D011487:Protein Conformation; D012795:Sialoglycoproteins / Q000097:blood*; D012967:Sodium Dodecyl Sulfate
D006021:Glycophorins; D046911:Macromolecular Substances; D012795:Sialoglycoproteins; D012967:Sodium Dodecyl Sulfate