Abstract
The number of binding sites for l-triiodothyronine in rat erythrocyte membranes was increased 2-fold by incubation at 37°C for 60 min. An increase of approximately 3-fold was found when the incubation was carried out at 50°C. The proteinase inhibitor phenylmethylsulfonyl fluoride abolished the effect. Similar increments in the number of binding sites were obtained by treatment of the membranes with proteinases. The K d values (0.09 · 10 −10 M and 3.6 · 10 −10 M for the high-affinity and the low-affinity binding sites, respectively) remained unchanged after the treatment, as did the free-SH group requirements, storage stability and stereospecificity. Our results suggest that endogenous proteolytic activity could be involved in the increase of the number of membrane latent sites for l-triiodothyronine.
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