Thermodynamic and kinetic properties of fatty acid interactions with rat liver fatty acid-binding protein.

@article{Richieri1996ThermodynamicAK,
  title={Thermodynamic and kinetic properties of fatty acid interactions with rat liver fatty acid-binding protein.},
  author={Gary V. Richieri and Ronald T. Ogata and Alan M Kleinfeld},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 49},
  pages={31068-74}
}
Fatty acid-binding protein from rat liver (L-FABP) binds 2 fatty acids (FA) per protein, in contrast to FABPs from adipocyte, heart, and intestine, for which binding and structural studies are consistent with a single FA binding site. To understand better the unique characteristics of L-FABP, we have carried out equilibrium binding and kinetic measurements of long chain FA using the fluorescent probes of free fatty acids (FFA), ADIFAB and ADIFAB2, to monitor the concentration of FFA in the… CONTINUE READING
17 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 17 extracted citations

Similar Papers

Loading similar papers…