Effects of nonenzymatic glycosylation and fatty acids on tryptophan binding to human serum albumin.

@article{Bohney1992EffectsON,
  title={Effects of nonenzymatic glycosylation and fatty acids on tryptophan binding to human serum albumin.},
  author={J P Bohney and Richard C. Feldhoff},
  journal={Biochemical pharmacology},
  year={1992},
  volume={43 8},
  pages={1829-34}
}
The effects of bound fatty acids and nonenzymatic glycosylation (NEG) on tryptophan binding to human serum albumin (HSA) were examined utilizing a rate of dialysis technique. HSA with 0, 1, 2, 3, or 5 mol of palmitate bound per mol of HSA was glycosylated in vitro to a level exceeding that seen in diabetes. NEG was not inhibited by fatty acids, suggesting that Lys-525, the primary site for NEG, is not an essential component of the principal sites for long-chain fatty acid binding to HSA… CONTINUE READING

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