A 13C NMR characterization of lysine residues in apolipoprotein B and their role in binding to the low density lipoprotein receptor.

@article{LundKatz1988A1N,
  title={A 13C NMR characterization of lysine residues in apolipoprotein B and their role in binding to the low density lipoprotein receptor.},
  author={Sissel Lund-Katz and J A Ibdah and Joseph Letizia and Manoj. T. Thomas and Michael C Phillips},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 27},
  pages={13831-8}
}
NMR spectroscopy of 13C-labeled human low density lipoprotein (LDL) has been employed to characterize the lysine (Lys) residues in apo B-100. Reductive methylation with [13C]formaldehyde converts up to two-thirds of the Lys to the dimethylamino derivative; this pool of Lys is exposed at the surface of the LDL particle. The [13C]dimethyl-Lys which are visualized exhibit resonances at chemical shifts of 42.8 and 43.2 ppm (pH 7.6) indicating that they exist in two different microenvironments; this… CONTINUE READING
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