Abstract

The activated cytoplasmic hydrocortisone-receptor complexes from both hormoneinsensitive (irresponsive to induction of glutamine synthetase by hydrocortisone) 7-day retina and hormone-sensitive (responsive to induction of glutamine synthetase by hydrocortisone) 12-day retina have been fractionated and identified by chromatography on phosphocellulose columns. The sedimentation patterns of these complexes are similar and indistinguishable from their nuclear counterparts. The retention pattern, salt extractability and the sedimentation properties of the nuclear complexes from both 7-day and 12-day retina also appear to be very similar. These results strongly suggest that the majority of the hydrocortisone receptors involved in the interaction with the nuclear acceptor sites are common to both the 7-day and the 12-day retina and that the factors controlling the age-related response of the retina to hydrocortisone lie at a step beyond the receptor-acceptor interaction.

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