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13C-N.M.R.-spectral study of the pH behavior of reductively [13C]methylated, glycophorin a glyco-octapeptides and a related glycopentapeptide

✍ Scribed by Kilian Dill; Robert E. Hardy; Ron L. Batstone-Cunningham; Marsha E. Daman; Bernard Ferrari; André A. Pavia

Publisher
Elsevier Science
Year
1984
Tongue
English
Weight
514 KB
Volume
128
Category
Article
ISSN
0008-6215

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✦ Synopsis

The pH dependence of the methylated compounds tri-L-Ser, labeled-carbon resonances of reductively [13C] glyco-octapeptide AM, asialoglyco-octapeptide . . AM, glyco-octapeptide AN, asialoglyco-octapeptide AN, and a glycopentapeptide was investigated. The results are discussed relative to those previously observed for reductively [13C]methylated, intact glycophorins AM and AN, and in terms of the mode of display of the MN blood-group specificities by these related glycoproteins. The results indicated that the cY-D-NeuAc groups appear to affect the pH-titration results of glyco-octapeptides AM and A N. Moreover, comparison of the pH-titration results for reductively [13C]methylated glyco-octapeptide AM and reductively [13C]methylated asialoglyco-octapeptide AM with those of a reductively [13C]methylated glycopentapeptide and reductively [13C]methylated tri+Ser indicated that the other carbohydrate residues present (cy-D-GalNAc and P-D-Gal) may also affect the pH-titration results. The reductive-methylation modification appears to affect the chemical shifts of the carbohydrate and peptide carbon atoms of the glycopentapeptide minimally. H&* HO OR OR OR 6 R = a-D-GalNAc+ *Indicates that the carbon atom is 90% 13C-enriched.

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