| Literature DB >> 1847389 |
H J Schoenfeld1, B Poeschl, J R Frey, H Loetscher, W Hunziker, A Lustig, M Zulauf.
Abstract
A fast and efficient method for medium scale purification of recombinant human tumor necrosis factor beta (rTNF-beta) from Escherichia coli cells is described. The purified rTNF-beta displayed biological activity similar to rTNF-alpha in a WEHI 164 cell cytotoxicity assay. The titration curve of rTNF-beta and elution profiles of rTNF-beta in gel filtration experiments were different from those of rTNF-alpha. However, light scattering and ultra-centrifugation studies showed that both cytokines have trimeric structures in solution at 0.5 mg/ml, with minor differences in the distribution of nontrimeric species. rTNF-beta bound to purified 55- and 75-kDa TNF receptors with high affinity. The binding of rTNF-beta to either receptor was analyzed on Scatchard plots and compared with that of rTNF-alpha.Entities:
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Year: 1991 PMID: 1847389
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157