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 substi...

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Veröffentlicht in:	American journal of hematology 1991-05, Vol.37 (1), p.51-52
Hauptverfasser:	Telen, Marilyn J., Le Van Kim, Caroline, Guizzo, Mary Lou, Cartron, Jean‐Pierre, Colin, Yves
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acids - analysis Asparagine - analysis Biological and medical sciences Blood Group Antigens - genetics Blotting, Western DNA - analysis DNA - genetics Erythrocytes - chemistry Erythrocytes - metabolism Fundamental and applied biological sciences. Psychology Genetic Variation - genetics Glycophorin - analysis Glycophorin - genetics Glycophorin - metabolism glycophorin C Glycosylation Humans Immune Sera Mutation - genetics Phenotype point mutation Polymerase Chain Reaction Serine - analysis Vertebrates: blood, hematopoietic organs, reticuloendothelial system Webb antigen
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Beschreibung
Zusammenfassung:	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.
ISSN:	0361-8609 1096-8652
DOI:	10.1002/ajh.2830370112