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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Richard-foy, H. Mercier-bodard, C. Baulieu, E. E. Radanyi, C. Secco-millet, C. |
| Abstract | In high-salt medium, cytosol from immature rat uteri displays two main high-affinity estradiol-binding peaks after ultracentrifugation in a sucrose gradient. The two components are the estradiol receptor which has a sedimentation coefficient of 5.5 S, and the alpha-fetoprotein which sediments at 4.5 S. The dissociation rate constants (k-1) of plasma alpha-fetoprotein-estradiol complexes measured at 0 degrees in the absence or presence of 0.4 M KCl were found to be 7 X 10(-5) and 8 X 10(-5) sec-1, respectively. The half-time of dissociation of these hormone-plasma protein complexes is 100-200 times more rapid than that of the estradiol-receptor complexes. These data led to the use of two 'differential dissociation' methods for the measurement of the hormone-binding protein complexes. In a high-salt cytosol, the charcoal technique measured selectively the receptor binding sites; the hydroxylapatite technique measured the sum of the alpha-fetoprotein plus receptor binding sites. Under these conditions, binding specificity studies provided evidence that alpha-fetoprotein is not a subunit of the receptor. This was confirmed by binding specificity studies in high-salt medium of the receptor separated from alpha-fetoprotein by ultracentrifugation. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 6 |
| Volume Number | 74 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1977-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Estradiol Metabolism Receptors, Estrogen Uterus Alpha-Fetoproteins Animals Binding, Competitive Cytosol Kinetics Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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