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Inhibition of Complement Fixation by Human Serum

II. The Activity of a -_1M Globulin and Rheumatoid Factor in Complement Fixation Reactions¹

From the Departments of Medicine and Biochemistry, Seton Hall College of Medicine and Dentistry, Jersey City, New Jersey

Abstract

Kinetic and static analyses of complement fixation (CF) reactions were carried out using EA, EA (human), solutions of human thyroglobulin-rabbit anti-thyroglobulin and latex particles coated with human -globulin (LPF II). Heated rheumatoid arthritis (RA) sera and N sera, rheumatoid factor (RF) and inhibitor (Ag-Ab)—a _1M-globulin isolated from RA sera—were tested for their effect on CF reactions.

Addition of RA serum and N serum to EA and gpC' delayed immune hemolysis. Preabsorption of the sera with solid heat denatured -globulin did not affect their inhibitory activity.

Inhibitor (Ag-Ab) was shown to delay lysis of EA by gpC'. The substance also inhibited CF by soluble antigen-antibody complexes, but CF reactions involving LPF II remained unaffected.

RF did not interfere with the lysis of EA by gpC'. This substance was also inactive in CF reactions involving soluble antigen-antibody complexes. RF, however, inhibited CF by LPF II, especially when preincubated with LPF II for 90 min at 56°C.

There was also a decrease in the latex fixation titer of RA sera when LPF II was preincubated with gp serum, suggesting some competition between RF and gpC' for sites of attachment on the -globulin molecule.

Footnotes

¹ This work was supported in part by Research Grant AM-07506 from the National Institute of Arthritis and Metabolic Diseases, Public Health Service and a grant from the New York State Chapter of the Arthritis and Rheumatism Foundation, Inc. Parts of this report have been presented at the 9th Interim Scientific Session, American Rheumatism Association, December 1962, Richmond, Virginia.

² Recipient of Senior Investigatorship of the Arthritis and Rheumatism Foundation.

³ Present address: Hôpital Lariboisiere, Paris, France.