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Immunoglobulin G preparations align unspecifically with all naturally occurring forms of the estradiol receptor, giving rise to soluble complexes of moderately increased sedimentation velocities. This interaction is not shown by the tryptic receptor fragment, which still contains the high affinity steroid binding site and the dimerization links of the native receptor.

Unspecific Interactions of Estrogen Receptors with Immunoglobulins and their Absence in the Tryptic Receptor Fragment