Abstract
Inactivation of homologous C3b by heated guinea pig, mouse and human serum was found to be much more rapid and complete at low ionic strength (0.037) than at μ = 0.15. The C3b inactivator in human and mouse serum was somewhat unstable to heating at 56°C. Heated guinea pig serum showed the greatest ability to inactive heterologous C3b, and human serum the least. Suramin (1 mg/ml) completely blocked homologous C3b inactivation by heated human, guinea pig and mouse serum, and 0.1 mg/ml was effective with mouse but not with human or guinea pig serum. Immune-adherence reactions with mouse C3 produced somewhat unstable hemagglutination patterns, which were improved by using ovalbumin in the buffer and minimizing EAC exposure to warm temperatures. A prozone phenomenon was frequently observed in immune-adherence hemagglutination with mouse C3, and less frequently with guinea pig and human C3.
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