The side chains responsible for the dimerization of the estradiol receptor by ionic bonds are lost in a 17 kDa fragment extending downstream from aa 303.

Fragments of 32, 26 and 17 kDa of the porcine estradiol receptor were prepared, all of which contain the ligand-binding site. While dimers of the 32 and 26 kDa fragments like those of intact receptor can be dissociated by protonation, the dimer of the 17 kDa fragment obtained by trypsination of the 26 kDa fragment is resistant to lowering the pH from 7.0 to 6.5 and below. Its dissociation can be achieved by 0.5 M MgCl2 at pH 7.0. All fragments are recognized by the MAB 13H2 in Western blots. The antibody also reacts with native receptor and the three fragments, both in their monomer and dimer states. The combining ratios of antibody with receptor, or its fragments, in the monomer and dimer states and the weakening of the estradiol-receptor bond by antibody attachment support the back to back and head to toe model of receptor dimers.