Specific 13C reductive methylation of glycophorin A. Possible relation of the N-terminal amino acid and the lysine residues to MN blood group specificities

The environment of the N-terminal amino groups of glycophorins AM and AN has been studied using 13C-NMR spectroscopy and pyrylium salts as amino-blocking agents. The extent of amino blocking was monitored by 13C-reductive methylation of the residual free amino groups. The pyrylium ions reacted with the N-terminal amino groups of the two glycophorins at almost identical rates, which is thought to indicate that the overriding steric bulk of the pyrylium salt may determine the rate of the reaction. The difference in the rates of modification of lysine residues of glycophorins AM) and AN by the pyrylium ions did indicate that there may exist an environmental difference around the lysine residues between the two glycophorins. This environmental difference may result from solution aggregation of the glycophorin A molecules or from some differences in the pKa values of the five lysine residues found in glycophorins AM and AN.

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13C-nuclear magnetic resonance study of glycophorins AM and AN modified with various pyrylium salts

Dill

Sutharchanadevi

et al. 1988

J Protein Chem

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One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla

Dill

Berman

et al. 1990

J Protein Chem

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One- and two-dimensional nuclear magnetic resonance (NMR) spectroscopy (at 11.7 Tesla) was used to gain some structural and spectral information about glycophorin AM, glycophorin AM tryptic glycopeptide, a related pentapeptide, and two related monoglycosylated pentapeptides. The protein spectral information suggests that the highly glycosylated N-terminus of glycophorin does not seem to possess a unique tertiary structure. Furthermore, the spectral information provided by the carbohydrate residues also indicates that there is no strong carbohydrate-protein interaction resulting in a unique tertiary structure. This result does not preclude any unique protein-carbohydrate interactions. For the small monoglycosylated pentapeptide containing alpha-D-GalNAc attached to Thr, a unique NOESY cross-peak was observed between the anomeric proton and the beta-proton of Thr. A cross-peak between the beta-proton of Ser and the anomeric proton was not observed for a related monoglycosylated pentapeptide containing alpha-D-GalNAc O-linked to Ser.

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31P nuclear magnetic resonance study of enzymatically phosphorylated glycophorin A

Culp

Dill

1986

J Protein Chem

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Specific 13C reductive methylation of glycophorin A. Possible relation of the N-terminal amino acid and the lysine residues to MN blood group specificities

Cited by 19 publications

References 33 publications

13C-nuclear magnetic resonance study of glycophorins AM and AN modified with various pyrylium salts

13C-nuclear magnetic resonance study of glycophorins AM and AN modified with various pyrylium salts

One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla

31P nuclear magnetic resonance study of enzymatically phosphorylated glycophorin A

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