title: Purification, characterization, and antitumor activity of nonrecombinant mouse tumor necrosis factor.
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 X 10(7) (L-cell assay in the absence of actinomycin D) and 1 microgram 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.
mesh_terms: D000818:Animals; D002845:Chromatography / Q000379:methods; D003208:Concanavalin A / Q000378:metabolism; D006023:Glycoproteins / Q000302:isolation & purification* / Q000627:therapeutic use; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D051379:Mice; D008815:Mice, Inbred Strains; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000378:metabolism; D012513:Sarcoma, Experimental / Q000188:drug therapy; D014409:Tumor Necrosis Factor-alpha
chemical_list: D006023:Glycoproteins; D014409:Tumor Necrosis Factor-alpha; D003208:Concanavalin A; D010447:Peptide Hydrolases