Studies on the homogeneity between high-and lowaffinity glucocorticoid receptor
The homogeneity between the high-and low-affinity glucocorticoid receptors(GR_H and GR_L)was testified by immunoaffinity chromatography using Mab N250(recognizing the immunogenic domain at the N terminal of GR_H)and Mab BuGR1(recognizing the DNA binding domain of GR_H).The specific binding peak of 0...
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Veröffentlicht in: | 中国人民解放军军医大学学报:英文版 1993 (2), p.125-131 |
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creator | 乐颖影 陆德如 徐仁宝 |
description | The homogeneity between the high-and low-affinity glucocorticoid receptors(GR_H and GR_L)was testified by immunoaffinity chromatography using Mab N250(recognizing the immunogenic domain at the N terminal of GR_H)and Mab BuGR1(recognizing the DNA binding domain of GR_H).The specific binding peak of 0.98μmol/L[~3H]triamcinolone acetonide(TA)was higher than that of 52.50nmol/L[~3H]TA.The re-sult suggests that the antigenic determinants of GR_L are similar to those of GR_H.ThecDNA of rat liver GR_H was introduced into GR_H-and GR_L-negative mouse fibroblast cellline E82.A3 by calcium phosphate coprecipitation.A number of clones which expressGR_H were selected with G418(400μg/ml).The results of radioligand binding assay indicatethat GR_H gene is expressed successfully and GR_L also may be encoded by GR_H gene. |
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ispartof | 中国人民解放军军医大学学报:英文版, 1993 (2), p.125-131 |
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language | eng |
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source | Alma/SFX Local Collection |
subjects | cell chromatography,affinity receptor-deficient receptors,glucocorticoid transfection |
title | Studies on the homogeneity between high-and lowaffinity glucocorticoid receptor |
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