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Erythrocyte webb‐type glycophorin C variant lacks N‐glycosylation due to an asparagine to serine substitution
Author(s) -
Telen Marilyn J.,
Le Van Kim Caroline,
Guizzo Mary Lou,
Cartron JeanPierre,
Colin Yves
Publication year - 1991
Publication title -
american journal of hematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.456
H-Index - 105
eISSN - 1096-8652
pISSN - 0361-8609
DOI - 10.1002/ajh.2830370112
Subject(s) - asparagine , serine , glycosylation , glycophorin , point mutation , amino acid substitution , mutation , gene , biochemistry , amino acid , chemistry , microbiology and biotechnology , genetics , biology , membrane , enzyme
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.