Ligand binding properties of human cellular retinoic acid binding protein II expressed inE. colias a glutathione‐S‐transferase fusion protein
- 26 April 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 321 (2-3), 163-168
- https://doi.org/10.1016/0014-5793(93)80100-9
Abstract
To test the hypothesis that 9-cis-retinoic acid is a ligand for cellular retinoic acid binding protein II (CRABPII), human CRABPII 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 retinoidsKeywords
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