N‐Terminal Amino Acid Sequence of Sialoglycoprotein D (Glycophorin C) from Human Erythrocyte Membranes

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Abstract
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, contains an average of about 12 O-glycosidically linked oligosaccharides and 1 asparagine-linked carbohydrate chain. An identical hexapeptide sequence occurring in 2 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.

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