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- W2056315770 abstract "Abstract The competitive effect of thyroxine on the interaction of 125 I-labeled p -iodobenzoate with human serum albumin was studied by equilibrium dialysis. At 30 °C and pH 7.4 in 0.06 m potassium phosphate buffer containing 0.7 m m EDTA, p -iodobenzoate is bound at a single binding site on human serum albumin with K = 1.8 × 10 6 m −1 , while thyroxine is bound to the protein at a single strong binding site, K 1 = 1.4 × 10 6 m −1 , plus a second set of several weaker binding sites. The calculated value of the association constant for thyroxine binding based on its competitive effect was less than, but in the same range as the value of K a as determined directly. Excellent agreement between the calculated competitive binding constant and K a for thyroxine was obtained when correction was made for interaction of thyroxine with the secondary set of binding sites. The results indicate that the p -iodobenzoate binding site is identical to the primary strong thyroxine binding site on human serum albumin." @default.
- W2056315770 created "2016-06-24" @default.
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- W2056315770 date "1979-12-01" @default.
- W2056315770 modified "2023-09-26" @default.
- W2056315770 title "Binding of 125I-labeled p-iodobenzoate to human serum albumin: Interaction with the primary thyroxine binding site" @default.
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- W2056315770 doi "https://doi.org/10.1016/0003-9861(79)90513-7" @default.
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