Abstract
The synthesis of biospecific adsorbents for the purification of the cytosol glucocorticoid receptor from rat liver is described. The binding properties of several dexamethasone spacer-derivatives were systematically studied. All agarose biospecific adsorbents tested, displayed specific binding properties. However, biospecific elution could only be obtained with long spacer chain derivatives (> 11 atoms). On the basis of its stability, its binding specificity and reversibility, a dexamethasone derivatized agarose was selected for the purification of the receptor. The purification procedure involves protamine sulfate precipitation followed by an affinity Chromatographic step with biospecific elution. The receptor-steroid complex is obtained in 15–20% yield and is about 7000-fold purified.
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