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Characteristics of Complement Fixation by Aggregated IgE¹

From the Department of Microbiology and Medicine, The Johns Hopkins University, School of Medicine at The Good Samaritan Hospital, Baltimore, Maryland

Abstract

Aggregated IgE fixed late components of complement (C), i.e., C3–C9, through an alternate pathway, bypassing C1, 4, and 2 whereas monomeric IgE did not. The aggregate, however, did not fix purified C3, suggesting that C3 activator system is involved in the reaction. On a weight basis, aggregated Fc had higher C-fixing activity than aggregated IgE, and aggregated F(ab')₂ was less active. The results indicated that structures essential for C fixation are present in the Fc portion of IgE molecules. A mild reduction and alkylation of IgE, which degraded structures involved in passive sensitization of monkey skin, did not affect the C-fixing properties of the protein.

Footnotes

¹ This work was supported by Research Grant AI-10060 from United States Public Health Service. This paper is Publication No. 45 from the O'Neill Laboratories, The Good Samaritan Hospital.