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The binding of 33 organic compounds to bovine serum albumin at pH 7.4 and 37°was studied using equilibrium dialysis. The affinity of the neutral molecules for the albumin is well correlated with their octanol-water partition coefficients. This is not true for molecules which are more than 50% ionized at pH 7.4. The constants in the linear free energy relationship derived for the 25 neutral molecules agree well with those obtained for other kinds of molecules. It is shown that the octanol-water and the iso-

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