[Detection and preliminary characterization of a particular estrogen-binding protein in the liver of male rats]статья

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[1] Smirnov A. N., Smirnova O. V., Rozen V. B. [detection and preliminary characterization of a particular estrogen-binding protein in the liver of male rats] // Biochemistry (Moscow). — 1977. — Vol. 42, no. 3. — P. 560–571. 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.

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