One-step 104-fold purification of transformed glucocorticoid receptor. Method for purifying receptors associated with Mr, ca. 90 000 heat-shock protein

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Abstract

Chromatography of rabbit glucocorticoid-receptor complexes in the absence of sodium molybdate on a Mono Q anion-exchange column induces the transformation of the receptor and allows the resolution of the transformed and non-transformed molecular species. These abilities were used to design a new purification scheme for the glucocorticoid receptor from rabbit liver in its transformed state. Microgram amounts of receptor were obtained using this single-step procedure in less than 2 h. The purification yield was 50-60%. Immunoblot experiments showed that the glucocorticoid receptor was present as an Mr≈ 94 000 polypeptide in these preparations and represented 20-30% of the eluted proteins as determined by densitometric scanning analysis of silver-stained sodium dodecyl sulphate polyacrylamide gels. Finally, the purified receptor was able to interact quantitatively with bulk DNA. © 1990.

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Denis, M., Blanchardie, P., Orsonneau, J. L., & Lustenberger, P. (1990). One-step 104-fold purification of transformed glucocorticoid receptor. Method for purifying receptors associated with Mr, ca. 90 000 heat-shock protein. Journal of Chromatography A, 508(C), 97–107. https://doi.org/10.1016/S0021-9673(00)91243-3

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