Purification, characterization, and antitumor activity of nonrecombinant mouse tumor necrosis factor.

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Abstract
Mouse tumor necrosis factor (TNF) was purified from serum through a series of steps, and each step was monitored for L-cell cytotoxicity in vitro and tumor-necrotizing activity in vivo. The two activities copurified and could not be dissociated. Purified mouse TNF has a specific activity of 2.2 .times. 107 (L-cell assay in the absence of actinomycin D) and 1 .mu.g causes necrosis of the standard TNF-sensitive sarcoma Meth A. TNF has a Mr of 39,000 .+-. 2000 by gel filtration and a Mr of 16,000-18,000 by NaDodSO4/PAGE. Both molecular weight forms display cytotoxic and necrotizing activities. TNF has a pI of 3.9 and is destroyed by trypsin, protease, elastase, and .alpha.-chymotrypsin but not by neuraminidase or papain. These characteristics of nonrecombinant mouse TNF clearly resemble those of recombinant human and mouse TNF.