A study was made on the fluorescence spectra of erythrosine, rose bengal and their protein complexes. In the visible region, the maximal emission of these colors shifted to a longer wavelength with increase of concentration of these colors. The fluorescence intensity decreased following the increase of concentration of these colors on the range of 4-10 X 10
-5M. This is a result of concentration quenching.
The addition of bovine plasma albumin to the buffered solution of erythrosine increased the fluorescence intensity of the buffered solution of erythrosine but decreased that of rose bengal.
In the addition of lower cancentration of bovine plasma albumin to the buffered solution of erythrosine, the fluorescence intensity increased at 508mμ and 549mμ or maximal emission over the pH range 5.2-10.0. However, at pH 12.0, the intensity increased in the addition of protein at 508 and 549mμ. Under the same condition of rose bengal, as the molar ratio of rose bengal to bovine plasma albumin decreased, the fluorescence intensity increased at 508mμ over the pH range 5.2-10.0. At pH 12.0, the intensity increased within tbe range of 5.0 X 10
-4 to 2.0 X 10
-2% but it started to decrease above 5.0 X 10
-2%. In the addition of bovine plasma albumin to the buffered solution of rose bengal, the determination at 570mμ or maximal emission showed that the fluorescence intensity increased in some cases or decreased in other cases over the pH range 5.2-12.0.
In the addition of lower concentration of casein to the buffered solution of erythrosine or rose bengal, the fluorescence intensity increased at 508mμ over the pH range of 5.2 to 10.0 but at pH 12.0 it started to decreased above 5 X 10
-2%. In the addition of casein to the buffered solution of erythrosine or rose bengal, the determination at 547mμ on the erythrosine and 570mμ on the rose bengal showed that the fluorescence intensity increased in some cases or decreased in many other cases.
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