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  • Title: Thyroxine-binding protein represents the major vitamin D-binding protein in the plasma of the turtle, Trachemys scripta.
    Author: Licht P.
    Journal: Gen Comp Endocrinol; 1994 Jan; 93(1):82-92. PubMed ID: 8138122.
    Abstract:
    Structural homology between the high-affinity thyroxine (T4)-binding protein (TBP) in the plasma of the turtle, Trachemys scripta, and vitamin D-binding proteins (DBP) of mammals prompted an investigation of plasma vitamin D binding in the turtle. Several lines of evidence indicate that the TBP represents the primary binding protein for 25-OH-cholecalciferol (D3) in the turtle plasma. D3-binding protein in whole plasma migrates in the same position as TBP by size-exclusion chromatography and polyacrylamide gel electrophoresis; it is electrophoretically distinct from sex hormone-binding proteins. D3 binding to purified TBP alone is enhanced (up to sevenfold) in the presence of plasma proteins, including albumin; with this correction, the D3-binding activity of plasma corresponds to expected TBP titers. Plasma selectively stripped of TBP by affinity chromatography and purified turtle albumin have only trace D3-binding activity. Variations in physiological state (thyroidal status, age, and sex) previously associated with variable T4 binding (and TBP levels) in T. scripta show correlated variability in plasma D3 binding. D3 binding is also highly correlated with T4 binding (r = 0.81; P < 0.001) for plasma samples taken from 30 adults representing 10 different species of Trachemys. D3 binding in plasma exhibits a high-affinity site (Ka = 2.3 x 10(8) M-1) and a second lower-affinity (Ka = 2 x 10(6) M-1), higher-capacity site; capacities are highly variable. Purified TBP has a comparable high affinity (Ka = 2.8 x 10(8) M-1), with a capacity close to 1 mol/mol. Binding of T4 and D3 are not competitive, indicating separate binding sites for the two ligands; in fact, T4 tends to enhance the affinity and the capacity for D3. A single protein in turtle plasma ("TBP/DBP") functions in the transport of two different hormones normally served by two distinct binding proteins (representing different multigene families) in mammals. These results have implications for the mediation of T4 effects on growth.
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