Conformational changes of bovine plasma albumin prior to the salting‐out of the protein in concentrated salt solution

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Abstract
By working at very low protein concentration (ca. 0.003%), it is possible to measure tryptophyl fluorescence intensity at 350nm (F350) of bovine plasma albumin (BPA) as a function of pH under precipitating conditions (acidic concentrated salt solutions). Under such conditions, distinct changes in F350 were seen before the starting of precipitation of BPA and no further changes in F350 over the precipitating pH range. Comparison of pH‐profiles monitored by F350 with those by solubility in the presence of various salts at various concentrations indicated that the change of solubility is observed after definite changes in conformation of the protein.