PMID: 3131591Apr 1, 1988Paper

Application of a mathematical model for two component receptor binding to two high affinity oestrogen binding sites in nuclei from DMBA rat mammary tumours

Journal of Steroid Biochemistry
E R ClarkS P Robinson


Saturation binding of [3H]oestradiol has been determined using exchange conditions, on nuclei from DMBA tumours from rats treated prior to sacrifice with oestradiol and tamoxifen alone or in combination. Application of a model to the binding data enabled the amounts (C2) and apparent dissociation constants (Kdapp) of a second lower affinity binding component to be determined as well as the amount of a higher affinity site (C1) and its dissociation constant (Kd1). Kdapp did not change significantly with any pretreatment but 2 h after oestradiol (5 micrograms) and after tamoxifen alone there was a significant decrease in Kd compared with control. It is suggested that the difference in Kd of the higher affinity binding sites in control and 2 h oestradiol treated animals may be due to the loss of an essential co-factor, possibly cytosolic, when nuclei are isolated in the absence of ligand.


Mar 29, 1977·European Journal of Cancer : Official Journal for European Organization for Research and Treatment of Cancer (EORTC) [and] European Association for Cancer Research (EACR)·R I NicholsonK Griffiths
Mar 15, 1978·Biochemical and Biophysical Research Communications·H ErikssonJ H Clark
Nov 1, 1980·Journal of Steroid Biochemistry·D D Keightley, N A Cressie
Jan 1, 1983·Breast Cancer Research and Treatment·J H ClarkW B Panko
Jan 1, 1980·Journal of Receptor Research·C S Watson, J H Clark
Dec 1, 1981·Journal of Steroid Biochemistry·J H Clark, B M Markaverich

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Aug 1, 1993·The Journal of Steroid Biochemistry and Molecular Biology·S Dove, H Schönenberger
Jan 1, 1996·Acta Oncologica·K G Hofer
Jan 1, 1993·Acta Oncologica·S E StrandJ Tennvall

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