Lack of binding of human C3, in its native state, to C3b receptors.
1981; American Association of Immunologists; Volume: 127; Issue: 4 Linguagem: Inglês
10.4049/jimmunol.127.4.1329
ISSN1550-6606
AutoresMartin R. Berger, T A Gaither, C H Hammer, Martin Frank,
Tópico(s)Coagulation, Bradykinin, Polyphosphates, and Angioedema
ResumoTo understand better the role of C3 in opsonization, we investigated the binding of purified C3 and C3b to C3b receptors. To ensure that only physiologically relevant binding would be detected, we assayed the ability of isolated proteins to inhibit formation of rosettes between EA(lgM)C4b3b and normal, viable human polymorpho- nuclear leukocytes. Freshly prepared C3, with specific hemolytic activity equal to that of serum, was capable of only 30% inhibition at
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