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Positive cooperativity of the estrogen receptor

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)
The equilibrium (/sup 3/H) estradiol binding by the partially purified estrogen receptor from calf uteri was measured at 25 C. The Scatchard plot of the binding data showed a convex curve characteristic of positive cooperativity and a Hill coefficient of 1.58 +- 0.21, at receptor concentrations of 1 to 10 nm. Below a receptor concentration of 0.3 nm the Scatchard plot approached linearity, suggesting that the cooperative interactions are dependent upon a monomer-dimer equilibrium. Trypsin pretreatment of the receptor resulted in a loss of dimer formation and of the cooperative interactions. The positive cooperative characteristics of the estrogen receptor were shown not to be produced by receptor inactivation, failure to complete the (/sup 3/H) estradiol-receptor equilibrium reaction, or radioimpurity of the (/sup 3/H) estradiol. These findings indicate that the activated 5S estrogen receptor is a homodimer and that is formation is associated with a positive cooperative estradiol-binding reaction.
Research Organization:
Univ. of Rochester School of Medicine and Dentistry, New York
OSTI ID:
6122376
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 78:8; ISSN PNASA
Country of Publication:
United States
Language:
English