Affinity purification of retinoic acid-binding proteins using immobilized 4-(2-hydroxyethoxy)retinoic acid.

@article{Chapman1990AffinityPO,
  title={Affinity purification of retinoic acid-binding proteins using immobilized 4-(2-hydroxyethoxy)retinoic acid.},
  author={J. M. Jun. Chapman and R. W. Jun. Curley},
  journal={Protein expression and purification},
  year={1990},
  volume={1 1},
  pages={
          63-9
        }
}
  • J. Chapman, R. Curley
  • Published 1 September 1990
  • Biology, Medicine
  • Protein expression and purification
An affinity chromatographic matrix that purifies cellular retinoic acid-binding protein to near homogeneity from rat testes cytosol has been developed. The three-step procedure includes an acid precipitation, a batch treatment with CM Bio-Gel, and affinity chromatography on 4-(2-hydroxyethoxy)retinoic acid coupled to epoxy-activated Sepharose 6B. The binding protein was purified approximately 8500-fold based on total soluble testicular protein and with a recovery in excess of 80%. In addition… Expand
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