Abstract
Extensively purified human IgM protein was digested with trypsin. One of the resultant split-fragments, was found to have a mol. wt of about 12,000 and strong chemotactic activity on rabbit peritoneal neutrophils. This chemotactic substance proved to be derived from the Fc portion of IgM, and not from (Fab) 2μ or Fabμ. (Fab) 2μ, Fabμ, (Fc) 5μ and unchanged IgM, which are produced from tryptic digestion of IgM, were shown to be devoid of chemotactic activity.
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