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Purification by affinity chromatography and immunological characterization of a 110kDa component of the chick oviduct progesterone receptor.
A 110kDa component of the chick oviduct progesterone receptor (PR) has been purified to homogeneity according to electrophoretic criteria and specific activity (assuming one progestagen-binding site/110kDa). The procedure involved affinity chromatography of 0.3 M-KCl-prepared cytosol, followed by DE...
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| Hoofdauteurs: | , , , , , , , , |
|---|---|
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
1984
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1153269/ https://ncbi.nlm.nih.gov/pubmed/6712592 |
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