Abstract
Corticosteroid Binder IB (20– 26Å) is the sole activated glucocorticoid-receptor complex in rat kidney cortex and represents a portion of the activated hormone-receptor complexes in liver cytosol. Binder II (50–60Å) is the major activated species formed in vitro in liver cytosol. If kidney cytosol prelabelled with [3H]triamcinolone acetonide [TA] is mixed 1:1 with liver cytosol preincubated with unlabelled TA and heat activated (25°C, 30 min), only Binder IB is formed, a typical kidney pattern. Addition of TA labelled kidney cytosol to liver cytosol prelabelled with [3H]TA during activation (25°C, 30 min) does not increase the proportion of Binder IB formed relative to Binder II when compared to a liver control. These experiments indicate that Binder IB is not derived from the activated Binder II by limited proteolysis.
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