Expression of cellular retinoic acid binding protein (CRABP) in Escherichia coli. Characterization and evidence that holo-CRABP is a substrate in retinoic acid metabolism.

@article{Fiorella1991ExpressionOC,
  title={Expression of cellular retinoic acid binding protein (CRABP) in Escherichia coli. Characterization and evidence that holo-CRABP is a substrate in retinoic acid metabolism.},
  author={P D Fiorella and Joseph L Napoli},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 25},
  pages={16572-9}
}
Cellular retinoic acid binding protein (CRABP) has been expressed efficiently in Escherichia coli from the cDNA of bovine adrenal CRABP and characterized, especially with respect to affinity for endogenous retinoids and a role for it in retinoic acid metabolism. The purified E. coli-expressed CRABP was similar to authentic mammalian CRABP in molecular weight (approximately 14,700), isoelectric point (4.76), absorbance maxima (apo-CRABP, 280 nm; holo-CRABP, 350 and 280 nm with the ratio A350… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 32 extracted citations

References

Publications referenced by this paper.

Chemistry and Biology of Synthetic Reti- mids (Dawson

  • J. L. Napoli
  • 1990

Similar Papers

Loading similar papers…