Fischer W, Bauer W, Feigel M
Eur J Biochem. 1987 Jun 15;165(3):647-52. doi: 10.1111/j.1432-1033.1987.tb11489.x.
The native lipoteichoic-acid-like amphiphile from Bifidobacterium bifidum subspecies pennsylvanicum and its basic glycan moiety, obtained by alkaline hydrolysis, were studied by 1H-, 13C-, and 31P-NMR, DEPT (distorsionless enhancement by polarization transfer), 1H-1H correlation spectroscopy and 13C-1H shift correlation NMR spectroscopy. The results are consistent with the structure elucidated by chemical analysis (Fischer, W., preceding paper in this journal): (formula; see text) and establish the structures of the repeating units independently. In addition to characteristic shifts in the 13C-NMR spectrum, the sites of phosphodiester and alanine ester bonds are also manifest in the 1H-NMR spectrum. Substitution of the glycerophosphate residues can be recognized in the 31P-NMR spectrum also.