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PMID: 170917 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Studies on sex-organ development. Isolation and characterization of an oestrogen receptor from chick Müllerian duct.

The Biochemical journal ·Vol. 150 ·No. 2 ·1975-08-00 ·Pages 183-90

Teng CS, Teng CT

Abstract

An oestradiol-binding macromolecule was observed in the left Müllerian duct of the 15-day female chick embryo. The embryonic receptor binds oestradiol with a high affinity and low capacity, having a Kd of 3.2 X 10(-9)M and a maximal number of sites of 5.45 fmol/10(6) cells in the left Müllerian duct. The receptor is protein in nature, as suggested by its susceptibility to proteolysis; in addition, it is organ- and steroid-specific. Judging by glycerol-gradient analysis, the hormone receptors in the cytosol are present in 8S and 4.5S forms, and the 8S form could be dissociated into a 4.5S form in the presence of 0.5M-KCl. A 4.5-6S receptor could be extracted from the nuclei. Under physiological salt conditions, the embryonic receptors bind to DNA-cellulose and can be eluted when the salt concentration is increased to 0.5M-KCl. Determination by isoelectric focusing indicates that the isoelectric point is 5.8 for the 8S and 6.9 for the 4.5S receptor.

MeSH Terms
Animals Binding Sites Binding, Competitive Cell Nucleus/metabolism Centrifugation, Density Gradient Chick Embryo Chromatography, Affinity Estradiol/metabolism Female Kinetics Mullerian Ducts/metabolism Protein Binding Proteins/isolation & purification,metabolism Receptors, Cell Surface
Chemicals
Proteins Receptors, Cell Surface Estradiol
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Teng C S
Teng C T
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40 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1500183
Published
1975-08-00
Pages
183-90
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1165724
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1500183 PMC Full Text View journal details
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