Abstract
The rotational diffusion of complexes of human serum albumin (HSA) and bovine serum albumin (BSA) with neutral surfactant Triton X-100 is study by analyzing the polarized tryptophan fluorescence and its parameters are determined (rotational relaxation time, diffusion coefficient, effective radius). Similarities in the solubilization of both proteins are revealed: an effective solubilization BSA and HSA in solutions containing neutral surfactant Triton X-100 is achieved at concentration of the latter of 0.3 mM, slightly greater than its critical micelle concentration (0.25 mM), with the most significant effect taking place at pH 5.0, a value close to the isoelectric points of the proteins.
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