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Tumor necrosis factor (TNF) has been reported to exhibit procoagulant activity. To examine this, we determined the total TNF recovered from rat, mouse, and human tumor cells by a method involving heat lability with dextran sulfate and magnesium ion. The method is demonstrated by recovery of biologically active mouse TNF from non-biotinylated and biotinylated hybridomas. Recombinant rat TNF (rTNF) was made by fusion of rat pro-TNF with the Escherichia coli expression plasmid, pTL1. rTNF is heat labile, and is immunologically identical to endogenous TNF. The procoagulant activity of rTNF was tested using a monocyte-dependent procoagulant assay. In all assays tested, rTNF was more potent than native murine TNF. In these assays the relationship between TNF and procoagulant activity was proportional, and the two parameters were strongly correlated. With rTNF, time course experiments showed a time course for biotinylated material closely paralleling that for binding of TNF, which had been made heat-stable by the addition of dextran sulfate and magnesium. This suggests a limited pool of TNF-reactive biotin binding sites, and indicates the method to be useful in identifying sites for TNF. These data support the conclusion that TNF has procoagulant activity, and demonstrate a method for separating low molecular weight inactive TNF from active, conformationally restricted TNF.The second of
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