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Analysis of the oxidative modification of proteins by means of fluorescence and elastic scattering
Authors:Piskarev  I M  Samoilova  A I  Ivanova  I P
Institution:1.Skobeltsyn Institute of Nuclear Physics, Moscow State University, Moscow, 119991, Russia
;2.Nizhny Novgorod State Medical Academy, Nizhny Novgorod, 603950, Russia
;
Abstract:

The fluorescence of pure tryptophan and tryptophan residues in albumin is studied at an excitation wavelength of 288 nm. The range of wavelength registration is 280–380 nm. A broad fluorescence band at 350–355 nm and an elastic scattering line at 288 nm are observed in the spectrum measured at 90° relative to the primary beam. The fluorescence of pure tryptophan and tryptophan in albumin is greatly reduced under the impact of the plasma radiation of a spark discharge, while the elastic scattering peak remains unchanged within the limits of error. A comparison of the elastic scattering and fluorescence indicates that tryptophan loses its inherent property to fluoresce under an external influence. The structure of the other tryptophan levels remains unchanged.

Keywords:
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