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N-terminal N alpha-[13C]monomethylamino derivatives for the N-terminal serine and leucine residues of glycophorins AM and AN, respectively, were obtained by reductively 13C-methylating homozygous human erythrocytes (MM, NN). The 13C-labeled glycophorins, AM and AN, were then isolated. A unique structural state was observed in solution reductively 13C-methylated glycophorin AM that was not observed in glycophorin AM derived from 13C-methylated erythrocytes. We attribute this state to the fact that some of the glycophorin AM forms a head-to-head dimer when subjected to reductive 13 C-methylation in aqueous solution. The 13C chemical shift data and pH titration data for the N-terminal [13C]dimethylamino and [13C]monomethylamino groups of glycophorin AM and AN derived from reductively 13C-methylated erythrocytes were in agreement with the chemical shift and titration data previously obtained for the N-terminal [13C]dimethylamino groups of solution reductively 13C-methylated glycophorins and related glycopeptides and peptides and N-terminal [13C]monomethylamino groups of related glycopeptides and peptides.
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R D Carter, and
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