Abstract
An immunoabsorbent column was made with antibody to trypsinized human C5. This column removed the chemotactic activity from zymosan-activated serum as well as from C5a des-arg-enriched fractions. Anti-trypsinized C5-absorbed human serum was substituted for unabsorbed human serum in the chemotaxis under agarose system. This resulted in significantly reduced random neutrophil migration with a negligible effect on C5a des-arg or FMLP-directed migration. The results indicate that much of the random migration observed in the chemotaxis under agarose system is due to C5-derived peptides present in normal human serum.
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