Abstract
1. 1. Properties of cytoplasmic proteins that bind cortisol in embryonic chicken liver have been compared with those formed with corresponding proteins in adult rat liver. Comparison of their Chromatographic properties, sedimentation rate, ion-exchange and electrophoretic behaviour showed close similarities. 2. 2. Both embryonic chicken liver and adult rat liver cortisol-cytosol protein complexes are excluded from Sephadex G-25 column with the void volume; their sedimentation constant as judged by sedimentation rate in linear sucrose density gradients is about 4S. 3. 3. Cortisol-liver cytosol protein complexes either from chicken embryo or adult rat can be separated into three distinct zones upon ion-exchange chromatography on DEAE-Sephadex A-50 column. When subjected to linear sucrose density gradient analysis, each of these three cortisol-binding protein classes sedimented in the range between 3 and 5S. 4. 4. Agarose-gel electrophoresis ofcytoplasmic protein-cortisol complexes revealed in both cases one broad radioactivity zone at the cathodic part of the electrophoretogram. 5. 5. On the basis of the above data it can be concluded that cortisol binds to very similar if not the same cytoplasmic proteins in the liver of higher animals, no matter how diverse they are phylogenetically.
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