[Dependence of human serum albumin fluorescence spectrum on the excitation wavelength].

The parameters of fluorescence spectrum of human serum albumin in N and F forms and of its complex with sodium dodecylsulphate were studied as a function of excitation wavelength within a range of 220-307.5 nm. The spectral range of the influence of tyrosine emission on protein spectra is localized. The effect of a long-wave shift at red edge excitation is found and interpreted in terms of delayed dipolar relaxation. In transition of albumin from N to F form and in complex formation with sodium dodecylsulphate a significant increase in the red edge effect is observed.