Abstract
Abstract Normal human serum contains a chemotactic factor inactivator (CFI) that irreversibly inhibits the neutrophil chemotactic activity associated with fragments of C3 and C5, the C complex, and the bacterial chemotactic factor derived from Escherichia coli. Physicochemical features of CFI include the following: it is present in the pseudoglobulin fraction of serum, soluble in ammonium sulfate at 60% saturation, and elutes in at least two different zones in ion exchange chromatography and in Sephadex gel filtration. Electrophoretically CFI appears in positions of α- and β-globulins. CFI reacts in an enzymatic-like manner: the inactivation of chemotactic activity is progressive with time, is temperature-dependent, and is maximal at pH 7.3. CFI is heat labile, being destroyed at 56°C after ½ hr. Its activity is not blocked by 0.02 M EDTA, 0.02 M phenanthroline, soybean trypsin inhibitor, DFP or ε-aminocaproic acid. Caseinolytic activity and carboxypeptidase-B-like activity (measured by hydrolysis of hippuryl-l-arginine) are lacking in CFI preparations.
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