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- W1503878308 abstract "1.Suspensions of rat thymocytes were incubated at 4° or 37°, rapidly washed at 4° and a nuclear fraction prepared by density gradient centrifugation. At 37° nearly all of the corticosterone-binding protein was present in the nucleus, while at 4° approx. 13 was found in the cytoplasm. 2.By Sephadex filtration or coal adsorption, corticosterone binding to high-molecular-weight compounds could be shown in a 100 000 × g supernatant from sonicated cells. 3.This binding was abolished by incubation with proteases or thiol reagents. 4.The binding was unstable. The apparent dissociation constant of the corticosterone binding was 2–5 times greater than the dissociation constant of the binding to whole cells. 5.The molecular weight of the corticosterone-binding compound was at least 100 000, as determined by Sephadex filtration. 6.The affinity for corticosterone was highest between pH 7 and 8." @default.
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- W1503878308 date "1970-09-01" @default.
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- W1503878308 title "Studies of the glucocorticoid-binding protein from thymocytes" @default.
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- W1503878308 doi "https://doi.org/10.1016/0005-2795(70)90312-0" @default.
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