Abstract：
: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.
journal_name
Mol Cell Endocrinoljournal_title
Molecular and cellular endocrinologyauthors
Auricchio F,Rotondi A,Bresciani Fdoi
10.1016/0303-7207(76)90007-1subject
Has Abstractpub_date
1975-12-01 00:00:00pages
55-60issue
1eissn
0303-7207issn
1872-8057journal_volume
4pub_type
杂志文章abstract：:Transthyretin (TTR) is a plasma thyroid hormone (TH) binder that emerged from an ancient hydroxyisourate hydrolase by gene duplication. To know how an ancient TTR had high affinity for THs, molecular and TH binding properties of lamprey TTRs were investigated. In adult serum, the lipoprotein LAL was a major T3 binder ...
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pub_type： 杂志文章
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journal_title：Molecular and cellular endocrinology
pub_type： 杂志文章
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