白细胞介素8片段在大肠杆菌中表达及其功能研究

EXPRESSION OF IL-8 FRAGMENTS IN E.COLI AND THEIRFUNCTIONAL INVESTIGATIONS

利用ＤＮＡ重组技术在大肠杆菌中表达出白细胞介素８的Ｎ端４３氨基酸片段（ＩＬ８－Ｎ）和Ｃ端２４氨基酸片段（ＩＬ８－Ｃ），经过ＦＡＣＳ和趋化活性鉴定表明，ＩＬ８－Ｎ和ＩＬ８－Ｃ均能与中性粒细胞结合，其中ＩＬ８－Ｎ能部分封闭ＩＬ－８的趋化活性。

sing DNA recombinary、techniques,we expressed a N-terminal fragment containing 43amino acid and a C-terminal fragment containing 24 amino acid of human interleukin-8(IL- 8)inE.coli,namely IL8-N and IL8-C, respectively.FACS analysis showed that both of the IL8-Nand IL8-C could bind to the murine neutrophils. Bioassay revealed that only IL8-N could partlyblock the effect of Ieukocyte chemotaxis of recombinant human IL-8.