[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.
D006801:Humans; D011485:Protein Binding; D012709:Serum Albumin; D012967:Sodium Dodecyl Sulfate; D013050:Spectrometry, Fluorescence
D012709:Serum Albumin; D012967:Sodium Dodecyl Sulfate
Zavisimost' spektra fluorestsentsii syvorotochnogo al'buimina cheloveka ot dliny volny vozbuzhdaiushchego izlucheniia.