An electrophoretic analysis of the serum proteins in infectious mononucleosis Public Deposited

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  • Thirty-six sera from cases of infectious mononucleosis and 25 normal human serum specimens were studied by electrophoresis on cellulose acetate. The results indicated that: The mean concentration of total protein in the mononucleosis sera was significantly higher than that of the normal sera. In 15 of the 36 mononucleosis specimens the total protein concentration was above the range of the normals. The higher protein concentration was due entirely to increased amounts of the globulin fractions. The gamma globulin contributed most to the increase. Its mean concentration was above normal and in 29 of the 36 cases the gamma globulin level was above the range for the normal sera. With respect to the alpha-2 globulin, the mean concentration was slightly above that for the normals and in nine of the 36 sera the concentration was above the normal range. The mean concentration of the alpha-1 and beta globulins was slightly higher than the corresponding means for the normals. Twenty-two mononucleosis sera were studied by electrophoresis on cellulose acetate followed by elution of each separate fraction and testing of the eluates for agglutination of sheep erythrocytes. The gamma globulin fraction of 21 of the 22 specimens agglutinated the sheep cells. The alpha-2 globulin fraction of ten mononucleosis specimens also showed hemagglutination. Nine of these ten sera had an alpha-2 globulin content above the upper limit of normal (0.89 g/100 ml). These results indicated that the heterophile antibodies were present in the gamma globulin fraction in almost all cases and in the alpha-2 globulin in about half the cases. In experiments in which eight mononucleosis sera were absorbed with beef erythrocytes, complete removal of the heterophile antibodies was observed in four specimens while four others retained a low titer of 1:5. The significant reduction of the gamma globulin fraction in all eight cases and of the alpha-2 fraction in four cases after absorption, with no reduction in other fractions indicates that the heterophile antibodies are mainly in the alpha-2 and gamma globulin fractions of the serum protein. These experiments support the quantitative data of the cellulose acetate experiments and the results of the hemagglutination experiments with the separate protein fractions. Twelve mononucleosis sera and 12 normal sera were studied by immunoelectrophoresis in agar gel. In all 12 mononucleosis specimens an abnormal pattern was observed in the alpha-2 globulin zone One and sometimes two of the components showed precipitin arcs longer than in normal sera, extending into the beta-1 globulin zone. These arcs apparently represent one or more altered components of the alpha-2 globulin, appearing on immunoelectrophoretic plates as a population of molecules with a wider than normal range of electrophoretic mobilities. These molecules could very possibly represent the heterophile antibodies shown by other methods to be present in the alpha-2 globulin. A second observation not revealed by other methods was the fact that in nine of the 12 mononucleosis sera the beta-2M globulin arcs were more heavily stained and more distinct than in the normal sera used for comparison, when antibody against normal and mononucleosis serum was used. Since beta-2M globulin is a recognized antibody carrier, and in view of the observation made by Strannegard (45) that ox cell hemolysins migrated with the beta-2M globulin in mononucleosis sera, the above observation suggests that the increase in the gamma globulin fraction, observed in our electrophoretic analyses of 36 mononucleosis sera, was at least partly due to an increase in the beta-2M globulin, which is not distinguishable from the gamma globulin in electrophoresis on cellulose acetate.
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