Paper electrophoretic studies of glycoproteins in rheumatic fever.

TmCLASSIC REPORT by Longsworth et at. (1) in 1939 on serum protein fractionation by free electrophoresis included rheumatic fever as one of the febrile diseases that had been studied. Employing the same medium, Rutstein et at. (2) followed this work with a more detailed study of serum proteins in rheumatic fever and noted changes in total protein and gamma globulin concentrations. Shetlar and co-workers (3-5) employed chemical analytic technics in studies of serum polysaccharides in rheumatoid diseases and found significant changes in these conditions. In the comprehensive study of Kuhns and Crittenden (6), involving paper electrophoretic fractionation of serum proteins, glycoproteins, and lipoproteins in rheumatoid arthritis and associated rheumatoid diseases, a similarity was noted in the serum-glycoprotein patterns of rheumatoid arthritis and rheumatic fever. Subsequent work by Salt (7), Sunderman and Sunderman (8), and Stidworthy et at. (9) with serum protein and glycoprotein fractionation has resulted in the consensus that, in rheumatoid arthritis, serum proteins show decreased albumin with increased alpha-2 and gamma globulin fractions. Glycoprotein changes in rheumatoid arthritis and rheumatic fever were most marked by increased alpha-i and alpha-2 globulins (9). A review of the studies to date shows that most investigations have been focused on serum-protein changes encountered in rheumatoid arthritis and allied diseases. Consequently, it was felt that a study of serum glycoproteins in individuals diagnosed as having rheumatic fever might supply additional information of interest on the subject.