Abstract
Comprehensive analysis of fluorescence of albumin shows a weak fluorescence band at 430 nm, whose intensity exhibits a remarkable sensitivity to the presence of heavy ions in water. Using this fluorescence as a marker, as low as 10 pM concentration of lead can be routinely detected. Such a great sensitivity is explained in terms of electrostatic interactions in solution, which promote protein agglomeration. The latter is independently confirmed using dynamic light scattering measurements.
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