The Journal of Experimental Medicine
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The Journal of Experimental Medicine, Vol 127, 589-603, Copyright © 1968 by The Rockefeller University Press

ARTICLE

HETEROGENEITY OF RABBIT IGM ANTIBODY AS DETECTED BY C'1a FIXATION

Leon W. Hoyer M.D.1, Tibor Borsos Sc.D.1, Herbert J. Rapp Sc.D.1, and Wilton E. Vannier M.D.1

1 From the Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, and the Biology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20014

The C'1a-fixing properties of purified rabbit IgM anti-benzenearsonate antibody were determined. When tested with sheep erythrocytes to which hapten had been coupled by diazo linkage, the number of C'1a molecules fixed was 21% of the number of IgM antibody molecules bound to the erythrocyte surface. This was not due to loss of C'1a-fixing capacity during the purification procedure. Preparative electrophoresis of the antibody concentrated C'1a-fixing molecules in the anodal region so that antibody fractions with greater C'1a-fixing capacity were obtained. The demonstration that C'1a fixation is a property of a subpopulation of IgM molecules provides evidence for previously unrecognized µ-chain heterogeneity.

Submitted on November 2, 1967


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