Abstract
IT was shown1 that strips of immature calf uterus incubated in vitro in the presence of 10−9 M 3H-oestradiol-17β concentrate the hormone 400 per cent or more; about 80 per cent of the radioactivity in the tissue is found associated strongly but non-covalently with the nuclear fraction and consists of intact 17β-oestradiol; treatment of the nuclear fraction with 0.4 M KCl at pH 8.5, as already applied by us to rat2, solubilizes an oestradiol-macromolecule complex which sediments at about 5S; the macromolecule is protein, or at least the moiety binding the hormone is protein. A similar 5S oestrophilic component from calf uterus was obtained by Jungblut et al.3. Recent studies4–6 suggest that the 5S macromolecule originates from the 8–10S macromolecular component which binds 17β-oestradiol and is found in the high speed supernatant of uterus.
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References
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PUCA, G., BRESCIANI, F. Association Constant and Specificity of Oestradiol-receptor Interaction. Nature 223, 745–747 (1969). https://doi.org/10.1038/223745a0
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DOI: https://doi.org/10.1038/223745a0
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