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• W1978266284 abstract "High-affinity, limited-capacity 3,5,3′-triiodo-l-thyronine (T3)-binding sites were dectected by in vitro saturation analysis in cell nuclei from liver, gill, kidney, brain, and erythrocytes (RBC), but not spleen. The sites were extracted from the purified nuclei using 0.4 M NaCl and incubated with [125]T3 in the presence of 0.2 M NaCl. In all tissues T3 binding approached equilibrium after 18 to 48 hr of incubation at 4° and was reversible upon addition of excess unlabeled T3. The T3 association and dissociation rate constants (k+ and k−) were measured from the initial (4 hr) [125I]T3 association and dissociation rates for liver (k+ = 8.9 × 109 liters · mol−1 · hr−1; k− = 0.067 hr−1) and for RBC (k+ = 1.9 × 108 liters · mol−1 · hr−1; k− = 0.11 hr−1). The association constants (Kα) determined by saturation analysis were similar in all tissues investigated (average Kα = 2.8 × 109 liters · mol−1), except in RBC (Kα = 1.2 × 1010 liters · mol−1). The Kα values calculated from the k+k− ratio (1.4 × 1011 liters · mol−1 and 1.8 × 109 liters · mol−1 for liver and RBC, respectively) differed substantially from those determined by saturation analysis. This discrepancy is likely due to nonsaturable T3 binding by coextracted nuclear proteins in the assay medium, altering the estimated k+. The maximal binding capacity of the nuclear sites varied widely between tissues (liver, 250; gill, 130; kidney, 63; brain, 30; and RBC, 10 fmol. (mg DNA)−1; spleen, below detection). This distribution of binding sites is generally consistent with the limited data available for teleost tissue responsiveness to T3 and supports the hypothesis that the T3-binding sites are physiological T3 receptors." @default.
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• W1978266284 date "1988-01-01" @default.
• W1978266284 modified "2023-10-18" @default.
• W1978266284 title "High-affinity, limited-capacity triiodothyronine-binding sites in nuclei from various tissues of the rainbow trout (Salmo gairdneri)" @default.
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• W1978266284 doi "https://doi.org/10.1016/0016-6480(88)90054-8" @default.
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