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Properties of 19 S Antibodies in Complement Fixation

I. Temperature Dependence and Role of Antigen Structure¹

Department of Pharmacology, Tufts University School of Medicine, Boston Massachusetts

Abstract

With several antigen-antibody systems, C' fixation reactivity of whole serum and of separated 19 S and 7 S antibody components was examined. Antigens which did fix C' with appropriate 19 S antibodies included: bacterial lipopolysaccharides, cardiolipin, denatured DNA and adenosine conjugated to poly-L-lysine or to lysinerich histone. No C' fixation was observed with 19 S antibodies and hemocyanin or with adenosine-human serum albumin or adenosine-ribonuclease conjugates. Corresponding 7 S antibodies fixed C' with all of the above antigens. All 7 S antibodies reacted much more effectively at 4°C than at 37°C. In the systems in which 19 S antibodies did fix C', the ratio of reactivity at 4°C to that at 37°C was much lower than was the case with 7 S antibodies, with both human and rabbit antisera. In the reaction of anti-adenosine macroglobulins with adenosine conjugated to lysine-rich histones, an increase in the average number of adenosine molecules substituted on the histone was accompanied by a fall in the ratio of 4°C effectiveness to 37°C effectiveness. C' fixation with macroglobulin antibodies may require both an antigen of relatively large molecular volume and critically spaced repeating determinants on an antigen molecule.

Footnotes

Supported in part by Grant GB5606 from the National Science Foundation.

² Recipient of Public Health Service Predoctoral Award No. 1 F1 GM-34,938-01.

³ Present address: Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts.

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