A 62-kDa nuclear protein that transforms the goat uterine nonactivated estrogen receptor (naER) to nuclear estrogen receptor II (nER II) has been isolated and purified. This is being identified as the naER-transforming factor (naER-TF). The transformation is achieved through deglycosylation of the naER. It is observed that the naER-TF action on the naER introduces significant changes in the structural and functional features of the naER. The capacity of the naER to bind estradiol increases 8- to 10-fold, while its hormone binding affinity reduces to a considerable extent following its exposure to naER TF. There is a critical ratio in the concentration of the two proteins, the TF and the naER, that would ensure an optimum transformation process. The transformed naER is incapable of dimerization with the estrogen receptor activation factor(E-RAF).