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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Ligand binding properties of human cellular retinoic acid binding protein II expressed in E. coli as a glutathione-S-transferase fusion protein.

To test the hypothesis that 9-cis-retinoic acid is a ligand for cellular retinoic acid binding protein II ( CRABP II), human CRABP II was expressed as a glutathione-S-transferase fusion protein ( GST- CRABP II) and a single affinity purification step used to extract it from bacterial lysates. GST- CRABP II bound all trans-retinoic acid with high affinity (Kd 14.2 +/- 6.5 nM), but 9-cis-retinoic acid bound poorly. These studies suggest that 9-cis-retinoic acid is not a ligand for CRABP II. Their ease of purification makes GST-CRABP fusion proteins useful tools for ligand binding studies with different retinoids.[1]

References

  1. Ligand binding properties of human cellular retinoic acid binding protein II expressed in E. coli as a glutathione-S-transferase fusion protein. Redfern, C.P., Wilson, K.E. FEBS Lett. (1993) [Pubmed]
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