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[Detection and preliminary characterization of a particular estrogen-binding protein in the liver of male rats]статья
Дата последнего поиска статьи во внешних источниках: 28 мая 2015 г.
- Авторы: Smirnov A.N., Smirnova O.V., Rozen V.B.
- Журнал: Biochemistry (Moscow)
- Том: 42
- Номер: 3
- Год издания: 1977
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 560
- Последняя страница: 571
- Аннотация: Properties and isolation possibilities of an estradiol (E2) binding protein from male rat liver cytosol as possible estrogen receptor are studied. The protein is found to differ considerably in a number of characteristics from well-known receptor and non-receptor rat proteins, specifically binding estrogen. Equilibrium constant of E2-protein interaction is 1-10(8) M-1, the concentration of protein binding sites is 1.3 million per cell. Processes of E2 association with protein and the complex dissociation proceed with a very high rate. E2 and, at lesser degree, estrone, testosterone and 5-alpha-dihydrotestosterone compete for binding sites of protein with 3H-E2. Progesterone, corticosterone and a synthetic estrogen, hexestrol, denot compete. The protein studied is thermolabile and sensitive to the effect of pronase and sulfhydryl reagents. Characteristics of the protein are as follows: sedimentation coefficient–3.6S; Stockes’ radius–23–25 A; friction coefficients ratio–1.05–1.12; molecular weight–36000–39000. The protein is not revealed in the liver of female rats. Ammonium sulphate precipitation, gel filtration and ionic exchange chromatography made possible to obtain 50-fold purified protein preparation.
- Добавил в систему: Смирнов Александр Николаевич