Separation of two molecular forms of human estrogen receptor by hydrophobic interaction chromatography
- 1 January 1989
- journal article
- research article
- Published by Elsevier in Journal of Chromatography A
- Vol. 476, 455-466
- https://doi.org/10.1016/s0021-9673(01)93889-0
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Characterization of the nontransformed and transformed androgen receptor and heat shock protein 90 with high-performance hydrophobic-interaction chromatographyThe Journal of Steroid Biochemistry and Molecular Biology, 1988
- High-performance hydrophobic interaction chromatography as a means of identifying estrogen receptors expressing different binding domainsJournal of Chromatography A, 1988
- High-performance hydrophobic interaction chromatography of estrogen receptors and magnesium dependent protein kinase(S): Detection of two molecular forms of estrogen receptors in the presence and absence of sodium molybdateThe Journal of Steroid Biochemistry and Molecular Biology, 1988
- Progestin receptors from tissues either exhibiting or lacking estrogen response mechanisms : Comparison of conventional and high-performance liquid chromatography methodologyJournal of Chromatography A, 1987
- Characterization of estrogen receptors and associated protein kinase activity by high-performance hydrophobic-interaction chromatographyJournal of Chromatography A, 1987
- Estrogen receptor is associated with protein and phospholipid kinase activitiesBiochemical and Biophysical Research Communications, 1986
- High-performance hydrophobic-interaction chromatography of steroid hormone receptorsJournal of Chromatography A, 1985
- High-performance size exclusion chromatography as a rapid method for the separation of steroid hormone receptorsJournal of Chromatography B: Biomedical Sciences and Applications, 1984
- Monoclonal antibodies to human estrogen receptor.Proceedings of the National Academy of Sciences, 1980
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976