Erythrocyte Webb-type glycophorin C variant lacks N-glycosylation due to an asparagine to serine substitution.
We have analyzed part of the sequence of the human glycophorin C (GPC) gene carried by a Webb blood-group positive donor. Our results indicate that the lack of N-glycosylation of the variant GPC associated with the Webb phenotype is due to a point mutation resulting in an asparagine to serine substitution at amino acid position 8.
Telen
M J
MJ
Department of Medicine, Duke University Medical Center, Durham, North Carolina.
Le Van Kim
C
C
Guizzo
M L
ML
Cartron
J P
JP
Colin
Y
Y
D000596:Amino Acids / Q000032:analysis; D001216:Asparagine / Q000032:analysis*; D001789:Blood Group Antigens / Q000235:genetics; D015153:Blotting, Western; D004247:DNA / Q000032:analysis / Q000235:genetics; D004912:Erythrocytes / Q000737:chemistry / Q000378:metabolism*; D014644:Genetic Variation / Q000235:genetics; D006021:Glycophorins / Q000032:analysis / Q000235:genetics* / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D007106:Immune Sera; D009154:Mutation / Q000235:genetics; D010641:Phenotype; D016133:Polymerase Chain Reaction; D012694:Serine / Q000032:analysis*
D000596:Amino Acids; D001789:Blood Group Antigens; D006021:Glycophorins; D007106:Immune Sera; D012694:Serine; D001216:Asparagine; D004247:DNA