The Hageman factor substrates prekallikrein and plasminogen proactivator were found to generate chemotactic activity for human mononuclear cells upon interaction with Hageman factor fragments. This activity superimposed the elution profile of kallikrein and plasminogen activator after chromatography on SP Sephadex and Sephadex G-150 and was inhibited by incubation of both enzymes with the active-site serine-inhibitor diisopropyl fluorophosphate. The natural inhibitors of each active enzyme also functioned as chemotactic inactivators; thus α2-macroglobulin inhibited the chemotactic activity of kallikrein and plasminogen activator whereas C1 inhibitor inhibited only the chemotactic activity of kallikrein.
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Gallin et al. (1974) studied this question.