Abstract:
:Human thyroid hormone receptor (c-erb A protein) produced by Escherichia coli expression vector plasmid was purified sequentially using polyethylenimine precipitation of DNA, hydroxylapatite column chromatography, ammonium sulphate precipitation, Sephacryl S-300 gel filtration and mono Q-Sepharose column chromatography. These column procedures resulted in 41.3-fold purification of 3,5,3'-tri-iodo-L-thyronine (T3) binding activity over the initial E. coli extract. Purified protein as well as crude preparation showed high-affinity binding to T3. The c-erb A protein enriched by column purification was further purified by electroelution after electrophoresis. Rabbit antibody against the c-erb A protein was prepared and used for the Western blotting analysis. The antibody recognized c-erb A protein but not the bacterial proteins in crude E. coli extract. When partially purified rat hepatic nuclear thyroid hormone receptor was analysed, a 56 kDa receptor was specifically recognized by the antibody.
journal_name
J Mol Endocrinoljournal_title
Journal of molecular endocrinologyauthors
Ichikawa K,Hashizume K,Nishii Y,Takeda T,Kobayashi M,Suzuki S,Yamada Tdoi
10.1677/jme.0.0070123subject
Has Abstractpub_date
1991-10-01 00:00:00pages
123-9issue
2eissn
0952-5041issn
1479-6813journal_volume
7pub_type
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