| Literature DB >> 3493921 |
J A Schifferli, G Hauptmann, J P Paccaud.
Abstract
The classical pathway of complement is required for the adherence of soluble tetanus toxoid (TT)-human anti-TT complexes to erythrocytes. Using human C4-deficient serum we compared the capacity of the two forms of human C4 (C4A and C4B) to mediate this function: C4A was shown to be 1.5-fold more efficient than C4B. In contrast, haemolysis by C4B was 3.7-fold more efficient than by C4A. Such large differences suggest that both forms are complementary, and that C4A is preferentially involved in the processing of immune complexes in humans.Entities:
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Year: 1987 PMID: 3493921 DOI: 10.1016/0014-5793(87)81533-8
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124