| Autor: |
Aggarwal, B B, Kohr, W J, Hass, P E, Moffat, B, Spencer, S A, Henzel, W J, Bringman, T S, Nedwin, G E, Goeddel, D V, Harkins, R N |
| Zdroj: |
Journal of Biological Chemistry; February 1985, Vol. 260 Issue: 4 p2345-2354, 10p |
| Abstrakt: |
Human tumor necrosis factor (TNF) was purified to homogeneity from serum-free tissue culture supernatants of the HL-60 promyelocytic leukemia cell line induced by 4 beta-phorbol 12-myristate 13-acetate. The purification scheme consisted of controlled-pore glass and DEAE-cellulose chromatography, Mono Q-fast-protein liquid chromatography, and reverse-phase high performance liquid chromatography. The purified protein was homogeneous by the criteria of sodium dodecyl sulfate-polyacrylamide gel electrophoresis and NH2-terminal sequence analysis. The specific activity of purified tumor necrosis factor is approximately 10(8) units/mg. The protein has a molecular weight of approximately 17,000, an isoelectric point of 5.3, and contains two cysteines involved in a disulfide bridge. Approximately 50% homology between TNF and another cytolytic lymphokine, lymphotoxin, exists when the NH2-terminal 34 residues of TNF and internal sequence generated by tryptic, Staphylococcus aureus V8 protease, and chymotryptic digests of TNF are aligned with the complete amino acid sequence of lymphotoxin. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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