Stabilization, accurate determination, and purification of rat liver nuclear thyroid hormone receptor
- 1 February 1989
- journal article
- research article
- Published by Bioscientifica in Journal of Endocrinology
- Vol. 120 (2) , 237-243
- https://doi.org/10.1677/joe.0.1200237
Abstract
Rat liver nuclear thyroid hormone receptor lost 3,5,3′-tri-iodo-l-thyronine (T3)-binding activity with a half-life of 14 days, 4 h, 139 min, 62 min, 16 min or 6 min at 0, 36, 38, 40, 43 or 45 °C respectively, when present in crude nuclear extracts. Glycerol increased the half-life of the receptor during heat inactivation. Protection was reversible by removing the glycerol. The receptor was unstable at a pH below 6·0 or above 10·0. We also found a loss of the receptor activity during the separation of bound and free hormone using the resin test. Of several conditions tested for the separation of bound and free hormone, the addition of heated nuclear extract gave the most accurate estimation of bound hormone when using the resin test. Using these characteristics of the receptor, we purified the receptor to 1220 pmol T3-binding capacity/mg protein with a final yield of 14·6 μg/4 kg rat liver. Journal of Endocrinology (1989) 120, 237–243This publication has 3 references indexed in Scilit:
- Purification and characterization of rat liver nuclear thyroid hormone receptors.Proceedings of the National Academy of Sciences, 1987
- Interactions of the nuclear thyroid hormone receptor with core histones.Journal of Biological Chemistry, 1984
- Stability of Nuclear Triiodothyronine Binding SitesEndocrinology, 1977