Fatty acids and retinoids bind independently and simultaneously to beta-lactoglobulin.

@article{Narayan1997FattyAA,
  title={Fatty acids and retinoids bind independently and simultaneously to beta-lactoglobulin.},
  author={Murli Narayan and Lawrence J. Berliner},
  journal={Biochemistry},
  year={1997},
  volume={36 7},
  pages={1906-11}
}
beta-Lactoglobulin (Big) binds 1 mol of a fatty acid spin-label analog, 5-doxylstearic acid (5-DSA), per mole of protein with a dissociation constant Kd = 0.8 microM for the strongest binding site. There are also several weaker sites for this ligand. Blg saturated with either retinol or retinoic acid binds 5-DSA with essentially equal affinity (Kd = 0.6 and 1 microM, respectively). Palmitic acid and SDS displace bound 5-DSA from Blg. However, unlike palmitic acid, 5-DSA binding does not enhance… CONTINUE READING

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