摘要
肿瘤坏死因子是一种重要的炎性细胞因子 ,目前已知许多免疫疾病与之相关 ,为了抑制TNF的生物学活性 ,将可溶性TNFRII(sTNFRII)和人IgGFc分子通过柔性短肽相连 ,构建成一个嵌合蛋白 ,在大肠杆菌中进行表达 ,并获得了纯化蛋白。实验证明该嵌合蛋白能够自发形成聚合体 ,识别并结合TNF蛋白 ,同单体sTNFRII相比 ,对TNF的中和活性得到了较大的提高。
Tumor necrosis factor (TNF) is a key cytokine in immunology system and is related to many human diseases. In order to inhibit the activity of TNF, cDNA coding for soluble TNF receptor II (sTNFRII) and human IgG Fc were linked using a flexible hinge. This gene was expressed in E.coli as a chimeric protein and purified by metal chelate chromatography. The results show that the fusion protein exists in the physiological form as a dimer, has the ability to bind with TNF and inhibits the cytotoxicity of TNF on L929 cells. Contrasting to monomer sTNFRII, the chimeric protein has an improved bioactivity, and displays potential prospects for research and application.
出处
《生物工程学报》
CAS
CSCD
北大核心
2002年第2期178-181,共4页
Chinese Journal of Biotechnology
基金
国家 8 6 3高科技生物领域基金资助 (No .10 2 0 8 0 1 0 3)~~
