Covalent chromatography by thiol-disulfide interchange of the highly-purified non-transformed rat liver glucocorticoid-receptor
- 1 November 1985
- journal article
- research article
- Published by Elsevier in The Journal of Steroid Biochemistry and Molecular Biology
- Vol. 23 (5) , 593-597
- https://doi.org/10.1016/0022-4731(85)90009-3
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- Inactivation of unbound rat liver glucocorticoid receptor by N-alkylmaleimides at sub-zero temperaturesBiochimica et Biophysica Acta (BBA) - General Subjects, 1984
- Evidence for distinct sulfhydryl groups associated with steroid- and DNA-binding domains of rat thymus glucocorticoid receptorsBiochemistry, 1984
- Sulfhydryl-modifying reagents reversibly inhibit binding of glucocorticoid-receptor complexes to DNA-celluloseBiochemistry, 1984
- Purification of rat liver glucocorticoid receptor by affinity chromatography: Design of a suitable adsorbentThe Journal of Steroid Biochemistry and Molecular Biology, 1981
- Maximizing the purification of the activated glucocorticoid receptor by DNA-cellulose chromatographyBiochemical Journal, 1978
- Steroid Hormone ReceptorsPublished by Elsevier ,1976
- Assay of proteins in the presence of interfering materialsAnalytical Biochemistry, 1976
- The involvement of receptor sulphydryl groups in the binding of steroids to the cytoplasmic glucocorticoid receptor from rat thymusBiochimica et Biophysica Acta (BBA) - General Subjects, 1975
- [66] Covalent chromatography by thiol-disulfide interchangePublished by Elsevier ,1974
- Glucocorticoid receptors: Relations between steroid binding and biological effectsJournal of Molecular Biology, 1972