The conversion of human recombinant endothelial cell-derived IL-8 fusion proteins by thrombin / 中国免疫学杂志

ABSTRACT

By using genetic engineering techniques,we expressed in E.coli fusion proteins which con-tained human endothelial cell-derived IL-8 (EDhIL-8)、MS2 protein and different length of ?- galactosidase segments,named MS2-hIL-8、lac-hIL-8, lac-T-hIL-8 respectively.The lac-T-hIL-8 has a synthesized thrombin recognition site.Because there is a natural thrombin recognition sitewithin the EDhIL-8,thrombin can hydrolyze lac-hIL-8 and MS2-hIL-8 into natural hIL-8 ex-hibited biological activity,but has no effect on lae-T-hIL-8 which contained two recognition sitesfor thrombin.These results here indicated that the recognition of thrombin dependents on notonly the amino acid sequences of the substrates,but also the conformation formed by these aminoacids.