Heterogeneity of molybdate-stabilized, nontransformed glucocorticoid receptor from rat liver |
| |
| Authors: | T Nemoto Y Ohara-Nemoto M Ota |
| |
| Institution: | 1. Laboratory of Experimental Cancer Research (LECR), Department of Radiation Oncology & Experimental Cancer Research, Ghent University, Gent, Belgium;2. Department for Molecular Biomedical Research, VIB, Gent, Belgium;3. Department of Biomedical Molecular Biology, Ghent University, Gent, Belgium;4. Receptor Research Laboratories, Nuclear Receptor Lab (NRL), VIB Department of Medical Protein Research, Ghent University, Gent, Belgium;1. Institute for Diabetes and Endocrinology IDE, Helmholtz Munich, Ingolstaedter Landstr. 1, 857649 Neuherberg, Germany;2. Hospital for Special Surgery Research Institute, The David Rosenzweig Genomics Center, New York, NY, USA;3. Graduate Program in Physiology, Biophysics and Systems Biology, Weill Cornell Graduate School of Medical Sciences, New York, NY, USA;4. Graduate Program in Immunology and Microbial Pathogenesis, Weill Cornell Graduate School of Medical Sciences, New York, NY, USA;5. Metabolic Programming, TUM School of Life Sciences & ZIEL Institute for Food and Health, Gregor11 Mendel-Str. 2, 85354 Freising, Germany |
| |
| Abstract: | Nontransformed glucocorticoid receptor stabilized with sodium molybdate exists as the heterogeneous forms which have slight differences in net charges and sedimentation coefficients. These differences could be detected by sequential analyses with DEAE-Sephacel chromatography and glycerol gradient centrifugation. The heterogeneity in the nontransformed receptor appears to be caused by the association of an acidic component(s) with the transformed receptor. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
