Department of Chemistry, Clemson University, Clemson, SC 29631, USA
Abstract:
13C-n.m.r. spectral data for 13C reductively methylated intact homozygous and heterozygous glycophorins A were compared with the 13C-n.m.r. spectral data for the 13C reductively methylated homozygous and heterozygous N-terminal glycopeptides derived from the trypsin digest of glycophorin A. The results indicate that pronounced aggregation of this glycoprotein in solution does not affect the structural differences that we have previously observed for glycophorins AM and AN at and/or near the N-terminal amino acid. Moreover, the data suggest that two structural states exist for glycophorin AM.