Kinetic analysis of the nonenzymatic glycosylation of hemoglobin.

@article{Higgins1981KineticAO,
  title={Kinetic analysis of the nonenzymatic glycosylation of hemoglobin.},
  author={Paul J. Higgins and H. Franklin Bunn},
  journal={The Journal of biological chemistry},
  year={1981},
  volume={256 10},
  pages={
          5204-8
        }
}
Purification of glycated hemoglobin.
Characterization of unstable hemoglobin A1c complexes by dynamic capillary isoelectric focusing.
Identification and quantitation of N-(carboxymethyl)valine adduct in hemoglobin by gas chromatography/mass spectrometry.
  • J. Cai, H. Hurst
  • Chemistry, Biology
    Journal of mass spectrometry : JMS
  • 1999
TLDR
A sensitive, specific and reproducible method was developed for the quantitation of the hemoglobin (Hb) adduct N-(carboxymethyl)valine (CMV), and can detect CMV adduct in 5 mg globin samples with relative standard deviations less than 5%.
Some factors that influence the nonenzymatic glycation of peptides and polypeptides by glyceraldehyde
TLDR
The rate of reaction of glyceraldehyde with a series of peptides was found to be dependent on their amino acid composition, sequence, and chain length, and the presence of a histidine adjacent to the NH2-terminal at this site may facilitate the Amadori rearrangement.
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