Progestin-binding protein in human benign prostatic hypertrophy.
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概要
- 論文の詳細を見る
Cytosols from human benign prostatic hypertrophy contained progestin-binding components which bound to R 5020, ORG 2058 and progesterone in a high affinity fashion. Most of the protein bound to R 5020 was recovered in the precipitate with 0-30% saturation of ammonium sulfate. The R 5020-binding protein showed sedimentation coefficients of 3.6 S and 8.4 S, and was eluted in the void volume of a Sephadex G-200 column. This protein was clearly distinguished from the dihydrotestosterone-binding protein by its precipitability by ammonium sulfate, heat stability and susceptibility to delipidization. R 5020 and ORG 2058 binding were markedly inhibited by the addition of R 1881, therefore, most of the binding to progestin in cytosols from the benign prostatic hypertrophy seems to be also the sites for R 1881. Although nuclear extract by 0.4 M KC1 showed R 1881 binding, the extract did not contain the R 5020-binding protein, and this suggested that the progestin-bindingprotein observed in the cytosols does not seem to be the steroid receptor.
- 社団法人 日本内分泌学会の論文
著者
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Ito Masako
Department Of Anatomy School Of Medicine Fujita-gakuen Health University
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Kodama Takaomi
Department Of Urology Graduate School Of Medicine Chiba University
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Ito Haruo
Department Of Pharmacology Kanagawa Dental College
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Sato Ryoko
Department Of Cardiology Kanazawa Medical University
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SHIMAZAKI JUN
Department of Dermatology, School of Medicine, Chiba University
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