Autor: |
Collingwood TN; Department of Medicine, University of Cambridge, Addenbrooke's Hospital, UK., Sydenham M, Page MJ, Chatterjee VK |
Jazyk: |
angličtina |
Zdroj: |
FEBS letters [FEBS Lett] 1991 Oct 21; Vol. 291 (2), pp. 315-8. |
DOI: |
10.1016/0014-5793(91)81310-5 |
Abstrakt: |
We have overexpressed the human beta 1 thyroid hormone receptor in insect cells using a recombinant baculovirus to a level of 5-10% of total cellular protein. The recombinant protein migrates as a 50 kDa band by SDS-PAGE and Western blot analysis. The expressed receptor binds to L-T3 with a Kd of 1.3 +/- 0.4 x 10(-10) M and to thyroid hormone analogues with an affinity hierarchy of TRIAC greater than L-T3 greater than L-T4 greater than rT3. Gel retardation assays show highly specific receptor binding to a TRE which is modified by the presence of ligand and avidin-biotin complex DNA analysis shows a Kd of 6.2 +/- 2.0 x 10(-10) M for this interaction. These results indicate high level expression of hTR beta with authentic hormone and DNA binding properties. |
Databáze: |
MEDLINE |
Externí odkaz: |
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