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When the solution of bovine serum albumin (BSA) at pH 9 was heated at 65°C, new components (1'), (2), (3),were formed. Here the components (1'), (2), and (3) are modified monomer, dimer, and probably trimer, respectively. The component (1') was formed by the intramolecular sulf hydryl disulfide exchange reaction. Components (2) and (3) were formed by the intermolecular sulfhydryl disulfide exchange reaction. If appropriate amounts of anionic surfactant were added to BSA solution, the formation of component (1'), or the intramolecular exchange reaction, was prevented. It is known since earlier data that fatty acid anions prevent the denaturation of BSA. The cause found in this study was that the anionic surf actant prevented the formation of component (1' ). The minimum amounts of various surfactants to prevent the formation of component (1') were determined. The minimum molar ratio of surf actant/BSA was as follows : 5 for sodium tetradecyl sulfate and sodium palmitate, 6 for sodium tridecyl sulfate and sodium laurate, 7 for sodium dodecyl sulfate and sodium undecyl sulfate, 10 for sodium decyl sulfate, about 40 for sodium nonyl sulfate, and 28 for sodium hydrogen N lauroyl-L-glutamate (LS-11). These values are conventional measures of a relative affinity of surfactant to BSA, indicating that the affinity of LS-11 is between that of sodium decyl sulfate and sodium nonyl sulfate. The present method is useful in determining the relative affinity of any anionic surfactant to BSA.

Comparison of the Ability of Various Anionic Surfactants to Prevent Intramolecular Sulfhydryl Disulfide Exchange Reaction of Bovine Serum Albumin