| Autor: |
Kung, Hsiang-fu, Calvert, Ida, Bekesi, Eva, Khan, Fazlur R, Huang, Kuo-ping, Oroszlan, Stephen, Henderson, Louis E., Copeland, Terry D., Sowder, Raymond C., Wei, Shu-jing |
| Zdroj: |
Molecular and Cellular Biochemistry; August 1989, Vol. 89 Issue: 1 p29-35, 7p |
| Abstrakt: |
Human interleukin-2 (IL-2) is a lymphokine which is capable of activating lymphocytes and supporting the long-term in vitro growth of activated T cell clones. Recombinant human IL-2, expressed in either E. coli or cos cells, was shown to be phosphorylated by protein kinase C. Phosphorylated IL-2 synthesized in E. coli was analyzed by SDS-PAGE, reverse phase HPLC, and tryptic peptide mapping. The phosphorylated tryptic peptide was identified as the N-terminal fragment containing a single phosphorylation site at the serine residue at position 7. There was no difference in biological activity between non-phosphorylated and phosphorylated IL-2, as determined by a T cell growth assay. Although the physiological role of phosphorylation of IL-2 is unclear, IL-2 can be labeled with [?-32p] ATP and protein kinase C to a high specific radioactivity, and the synthesis of biologically active 32p-labeled IL-2 may be useful for receptor-binding studies of the cells containing low level of phosphoprotein phosphotases. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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