Auricchio F, Rotondi A, Bresciani F
Mol Cell Endocrinol. 1975;4(1):55-60. doi: 10.1016/0303-7207(76)90007-1.
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.
在切除卵巢的成年处女小鼠的乳腺胞质溶胶中，已检测到一种以特定方式结合3H标记的17β-雌二醇并在蔗糖梯度上8 - 10-S区域沉降的大分子成分。在4℃时，大分子-雌二醇复合物的解离常数为4.2×10^(-10)M。胞质溶胶中17β-雌二醇的结合位点为3.7×10^(-14)摩尔/毫克蛋白质。用不同酶孵育胞质溶胶表明，结合雌激素的胞质溶胶成分是蛋白质性质的。高温孵育以及一些但不是所有测试的巯基试剂会破坏结合活性。竞争研究表明，相对于其他甾体激素，该成分对雌激素具有特异性。结论是处女小鼠的乳腺胞质溶胶含有雌二醇受体。在怀孕和哺乳期，受体含量并非以特定方式增加，而是与乳腺总蛋白成比例增加。
