Abstract
AbstractStudies were carried out to confirm a previous report that the activity of migration inhibitory factor (MIF) was blocked by di‐isopropyl phosphorofluoridate (DFP), suggesting it acted as a protease. MIF was obtained by the stimulation of guinea pig lymphocytes with concanavalin A and the culture supernatants were chromatographed on Sephadex G‐100 gel columns. The MIF‐rich fraction was incubated with DFP or with other organophosphorus esterase inhibitors; the inhibitors were removed by dialysis, and the media were tested for MIF activity. The results, reported here, indicate that guinea pig MIF activity is not destroyed by treatment with serine esterase inhibitors.
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