Figure 7. Quenching of human serum albumin (hSA) fluorescence by F6. Fluorescence intensity obtained after equilibrating 5 [micro sign]M hSA or 5 [micro sign]M free L-tryptophan with various concentrations of F6. The solid line is a fit of the hSA fluorescence data to the binding isotherm given in Equation 7. The apparent Kdfor F6 = 160 +/- 11 [micro sign]M, and the Qmax= 1.05 +/- 0.038. The dotted line is a linear least-squares fit of the L-trytophan fluorescence data.

Figure 7. Quenching of human serum albumin (hSA) fluorescence by F6. Fluorescence intensity obtained after equilibrating 5 [micro sign]M hSA or 5 [micro sign]M free L-tryptophan with various concentrations of F6. The solid line is a fit of the hSA fluorescence data to the binding isotherm given in Equation 7. The apparent Kdfor F6 = 160 +/- 11 [micro sign]M, and the Qmax= 1.05 +/- 0.038. The dotted line is a linear least-squares fit of the L-trytophan fluorescence data.

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