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From the Departments of Medicine, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, and Baltimore City Hospitals, Baltimore, Maryland 21224
Abstract
Complement-fixing cryoproteins from rheumatoid synovial fluid were partially dissociated using preparative ultracentrifugation in a 15% sodium chloride, sorbitol gradient. Heavy-sedimenting fractions retained capacity to fix human complement and contained variable amounts of DNA. Using a modified micro-complement fixation procedure, additional complement fixation was obtained upon addition of denatured calf thymus DNA to fractions containing IgG or mixed IgG and IgM. There was little fixation with native DNA. Interaction of heat-aggregated human
G globulin with denatured DNA under assay conditions failed to give micro-complement fixation in excess of that by
G globulin alone, reducing the likelihood that a nonspecific reaction occurs between denatured DNA and
G globulin aggregates. These findings demonstrated the presence in rheumatoid synovial fluid cryoproteins of immunoglobulin with determinants specific for a site or sites on denatured DNA.
Footnotes
1 This work was supported by a research grant from the National Institutes of Health (AM 08827).
2 Recipient of Special Fellowship (F03 AM 18178) from the United States Public Health Service. Present address: The Good Samaritan Hospital, 5601 Loch Raven Blvd., Baltimore, Maryland 21239.
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