Glycophorins B and C from human erythrocyte membranes. Purification and sequence analysis.
We have developed methods for the preparative purification of two sialoglycoproteins (glycophorins B and C) from human erythrocyte membranes by high-performance ion exchange and gel permeation chromatography in the presence of Triton X-100. Glycophorin B was obtained without any detectable contaminants, and glycophorin C exhibited a purity of about 90-95%. The amino acid sequence of the intramembranous domain (residues 36-71) of glycophorin B was determined and found to be similar to that of the hydrophobic region of the major sialoglycoprotein (glycophorin A). The amino acid sequence of the hydrophobic domain (residues 49-88) of glycophorin C, that was also determined, agreed completely with the structure recently deduced from cDNA sequencing.
D000595:Amino Acid Sequence; D004247:DNA / Q000032:analysis; D004910:Erythrocyte Membrane / Q000032:analysis; D006021:Glycophorins / Q000235:genetics / Q000302:isolation & purification*; D006801:Humans; D011110:Polymorphism, Genetic; D012795:Sialoglycoproteins / Q000302:isolation & purification*
D006021:Glycophorins; D012795:Sialoglycoproteins; D004247:DNA