Palaszynski E W
Biochem Biophys Res Commun. 1987 Aug 31;147(1):204-11. doi: 10.1016/s0006-291x(87)80107-9.
Fragments of IL-1 beta were chemically synthesized and tested for biological activity as well as binding of radiolabelled peptides to the IL-1 receptor. A peptide from the extreme C-terminal region of IL-1 beta was found to antagonize intact, native IL-1 beta in the thymocyte bioassay. In addition, this C-terminal region peptide, when radiolabelled, can function as a ligand for the IL-1 receptor on murine cell lines and effectively compete with intact radiolabelled recombinant IL-1 beta.
白细胞介素-1β（IL-1β）片段经化学合成，并对其生物活性以及放射性标记肽与IL-1受体的结合情况进行了检测。在胸腺细胞生物测定中，发现来自IL-1β极端C末端区域的一种肽可拮抗完整的天然IL-1β。此外，这种C末端区域肽经放射性标记后，可作为小鼠细胞系上IL-1受体的配体，并能与完整的放射性标记重组IL-1β有效竞争。
