Structural studies of the M blood group determinant |
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Authors: | Ron L. Batstone-Cunningham Robert E. Hardy Kilian Dill |
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Affiliation: | Department of Chemistry, Clemson University, Clemson, SC 29631, USA |
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Abstract: | Structural studies of homozygous glycophorin AM were undertaken by monitoring the 13C methyl resonances of 13C reductively methylated glycophorin AM (contains five Lys residues, and the N-terminal Ser residues) in various forms of glycosylation. The results indicate that removal of the α-d-NeuAc residues does not affect the structure about the N-terminal Ser residue. However, removal of the fifteen O-linked oligosaccharide units results in a structural effect about the N-terminal Ser residue. Partial methylation experiments performed on native glycophorin AM and deglycosylated glycophorin AM indicate that methylation of the lysine residue(s) may influence the structure about the N-terminal Ser residue, especially in the case of deglycosylated AM. |
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Keywords: | Spectroscopy M blood group determinant carbohydrate residues glycophorin A |
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