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Clinical Chemistry, Vol 36, 1880-1883, Copyright © 1990 by American Association for Clinical Chemistry
MR Hubmann, MJ Leiner and RJ Schaur
Institute of Biochemistry, Karl-Franzens-University Graz, Austria.
The ultraviolet fluorescence emission spectra of sera from apparently healthy persons and of sera from cancer patients frequently show significantly different curve shapes. A biparametric fluorescence method has been developed to use these deviations to detect patients with malignant diseases (Clin Chem 1986;32:1974-8). However, the pathobiochemical reasons for these differences of diagnostic importance have thus far been unclear. To find a relevant explanation for the described effect, we focused our interest on human serum proteins, the materials mainly responsible for the intrinsic fluorescence of sera in this spectral region. Human sera of various protein compositions were selected according to their protein pattern, determined by cellulose acetate electrophoresis, and their intrinsic fluorescence properties were investigated. We found that the emission spectra of human sera were correlated with their relative protein compositions, albumin and alpha-2 globulins being the most significantly correlated with the fluorescence intensity ratios. Because increased percentages of alpha-2 globulins and decreased percentages of albumin frequently accompany malignancies, we suggest that this condition accounts for the differences between the emission spectra of sera from normal and cancer- bearing humans.
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