Association constant and specificity of oestradiol-receptor interaction.
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Biomedical subjects
Publications and source records attributed to F Bresciani.
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A macromolecular component binding 3H-labelled 17 beta-oestradiol in a specific manner and sedimenting in the 8-10-S region on sucrose gradient has been detected in the mammary gland cytosol of ovariectomized adult virgin mice. The dissociation constant of the macromolecule-oestradiol complex is 4.2 times 10(-10)M at 4 degrees C. The binding sites for 17beta-oestradiol of cytosol are 3.7 times 10(-14) mole/mg of protein. Incubation of cytosol with different enzymes suggests that the oestrogen-binding cytosol component is proteinaceous. The binding activity is destroyed by incubation at high temperatures and by some but not all SH-reagents tested. Competition studies show a specificity for oestrogens relative to other steroid hormones. The conclusion is that mammary gland cytosol of virgin mice contains oestradiol receptor. The receptor content does not increase in a specific manner during pregnancy and lactation but rather proportionally to total mammary gland protein.
The authors evaluate the positivity of the tumor markers CEA, AFP, TPA and ferritin among an homogeneous group of 500 patients suffering from a chronic hepatopathy and positive for HBsAg. The obtained results show a significant increase of TPA, AFP and Ferritin (70.4%, 20% and 24% respectively of the examined patients), while CEA is increased only in the 3.2%. The correlation between the positivity of these markers and possible evolution of the chronic hepatopathy is at present under investigation.
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