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N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.
The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing. The glycosylation sites were identified by a new procedure for the detection of the glycosylated derivatives released by Edman degradation. The fragment, comprising 47 residues, was found to contain an average of about 12 O-glycosidically linked oligosaccharides and one asparagine-linked carbohydrate chain. An identical hexapeptide sequence occurring in two regions of the glycopeptide provides evidence that it has developed by an internal gene duplication during evolution. In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
PMID: 7106126 [PubMed - indexed for MEDLINE]
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Cited by 10 PubMed Central articles
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Two individuals with elliptocytic red cells apparently lack three minor erythrocyte membrane sialoglycoproteins.
Anstee DJ, Parsons SF, Ridgwell K, Tanner MJ, Merry AH, Thomson EE, Judson PA, Johnson P, Bates S, Fraser ID.
Biochem J. 1984 Mar 1; 218(2):615-9.
[Biochem J. 1984]
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Individuals lacking the Gerbich blood-group antigen have alterations in the human erythrocyte membrane sialoglycoproteins beta and gamma.
Anstee DJ, Ridgwell K, Tanner MJ, Daniels GL, Parsons SF.
Biochem J. 1984 Jul 1; 221(1):97-104.
[Biochem J. 1984]
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Abnormal minor human erythrocyte membrane sialoglycoprotein (beta) in association with the rare blood-group antigen Webb (Wb).
Reid ME, Shaw MA, Rowe G, Anstee DJ, Tanner MJ.
Biochem J. 1985 Nov 15; 232(1):289-91.
[Biochem J. 1985]
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