Abstract
The ultraviolet fluorescence emission spectrum of bovine serum albumin was altered when free fatty acid (FFA) was added to the protein. This occurred when FFA was taken up from aqueous soap solutions, n-heptane solutions, rat epididymal fat pads, or fat emulsions undergoing enzymatic hydrolysis. As the molar ratio of FFA to albumin increased, the maximum emission was shifted to a shorter wave length and the fluorescence intensity was decreased. The blue shift did not exceed 7 mμ, and the maximum reduction in fluorescence intensity was less than 50% even when the molar ratio of FFA to albumin was high. Qualitatively similar results were obtained with FFA of 6–22 C atoms, but smaller effects occurred when FFA of less than 10 C atoms were used. FFA produced little or no change in the fluorescence intensity when the pH was less than 5.5 or greater than 10. FFA produced changes in the fluorescence spectrum of porcine albumin but had little effect on that of human, rabbit, equine or canine albumins.
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