Abstract
Blood plasma albumin (bovine serum albumin, BSA) interaction with a biologically active reagent 4-hydroxy-2-methylquinoline (4H2MQ) has been studied using fluorescence spectroscopy methods (steady state, synchronous, excitation/emission matrix, 3D spectra). With the addition of 4H2MQ, no changes in the spectral characteristics of BSA (fluorescence emission intensity and λmax position) are observed; only the symmetry of the BSA emission spectrum is changed and the full width at half maximum is decreased. The analysis of synchronous and 3D fluorescence spectra showed the existence of three emitting species in this system, which could be a result of changes in the fluorescence and photochemical properties of 4H2MQ.
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