Loading...
Please wait, while we are loading the content...
Similar Documents
Photoaffinity labelled rat androgen-binding protein and human sex hormone steroid-binding protein bind specifically to rat germ cells.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Felden, Franck Guéant, Jean Louis Ennya, A. Gérard, Anne Frémont, Sophie Nicolas, Jean Paul Gérard, H. |
| Copyright Year | 1992 |
| Abstract | A specific receptor with high affinity for rat androgen-binding protein (rABP) was identified in isolated adult rat germ cells and in the corresponding plasma membrane-enriched preparations. Binding was reversible and time-dependent, with maximum relative binding after 40 min at 4 degrees C; it was pH-dependent, with maximum binding at pH 6-8. Unlabelled rABP and human sex steroid-binding protein (hSBP), but not lactotransferrin, serotransferrin, asialofetuin, fetuin or bovine serum albumin, competed with labelled rABP for binding sites on isolated germ cells. Scatchard analysis revealed a single class of binding site with apparent dissociation constant (Kd) values of 0.78 +/- 0.04 nM and 0.97 +/- 0.05 nM in intact germ cells and plasma membrane preparations respectively. A Kd of 1.72 +/- 0.12 nM for hSBP showed that the receptor binding site was effective for both androgen-carrier molecules. Labelled rABP incubated with solubilized germ cell membrane fractions at pH 7 formed a complex excluded from Superose 6B mini-gels; this complex was not formed at pH 3. The receptor complex was also abolished in the presence of a 100-fold excess of either unlabelled rABP or unlabelled hSBP, or in the presence of 20 mM EDTA. These results suggest that the plasma membrane of rat germ cells contains a receptor which selectively binds rABP and hSBP. |
| Starting Page | 39 |
| Ending Page | 46 |
| Page Count | 8 |
| File Format | PDF HTM / HTML |
| PubMed reference number | 1515024 |
| Journal | Medline |
| Volume Number | 9 |
| Issue Number | 1 |
| Alternate Webpage(s) | https://jme.bioscientifica.com/downloadpdf/journals/jme/9/1/jme_9_1_005.pdf |
| Alternate Webpage(s) | https://doi.org/10.1677/jme.0.0090039 |
| Journal | Journal of molecular endocrinology |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
