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Research Article Free access | 10.1172/JCI106493
Department of Medicine, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
Department of Medicine, Baltimore City Hospitals, Baltimore, Maryland 21224
Find articles by Marcus, R. in: JCI | PubMed | Google Scholar
Department of Medicine, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
Department of Medicine, Baltimore City Hospitals, Baltimore, Maryland 21224
Find articles by Townes, A. in: JCI | PubMed | Google Scholar
Published February 1, 1971 - More info
A significant portion of a complement-fixing activity found in the synovial fluid of patients with rheumatoid arthritis, and previously implicated as a possible cause of the low synovial fluid complement levels in these patients behaves as a high solubility cryoprotein. Analysis of rheumatoid synovial fluid cryoproteins has revealed mixed immunoglobulins, bound complement components, fibrinogen, DNA, and rheumatoid factor.
Sorbitol density gradient studies on whole synovial fluid before and after removal of this activity has shown that the complement-fixing activity migrates in the 19S and heavier regions and that portion is removed with cryoprecipitation. Cryoproteins found in nonrheumatoid synovial fluid are generally devoid of complement-fixing activity and predominantly contain fibrinogen. DNA and IgG are also present, with IgG occurring significantly less frequently than in rheumatoid cryoproteins. These findings are discussed in relationship to recent studies demonstrating the presence of complement-fixing antibody to denatured DNA in rheumatoid cryoproteins.
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