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Expression of biologically active recombinant ferret (Mustela putorius furo) interleukin-8 from Escherichia coli
Makoto Nakata1, Yu Kozue, Takuya Itou
1Nihon University Veterinary Research Center, 1866 Kameino, Fujisawa, Kanagawa 252-8510, Japan.
The authors expressed recombinant ferret interleukin-8 protein (rfrIL-8) in Escherichia coli as a glutathione-S-transferase fusion protein. Western blot analyses revealed that anti-ovine IL-8 antibody reacted with rfrIL-8 at 10 kDa. To confirm that the rfrIL-8 was biologically active, the authors examined chemotaxis and respiratory burst activity of ferret polymorphonuclear blood cells (PMNs) exposed to rfrIL-8. The rfrIL-8 strongly induced chemotactic and respiratory burst activities in a statistically significant manner as compared with a negative control. Thus, the authors were able to successfully express biologically active rfrIL-8.
The authors expressed recombinant ferret interleukin-8 protein (rfrIL-8) in Escherichia coli as a glutathione-S-transferase fusion protein. Western blot analyses revealed that anti-ovine IL-8 antibody reacted with rfrIL-8 at 10 kDa. To confirm that the rfrIL-8 was biologically active, the authors examined chemotaxis and respiratory burst activity of ferret polymorphonuclear blood cells (PMNs) exposed to rfrIL-8. The rfrIL-8 strongly induced chemotactic and respiratory burst activities in a statistically significant manner as compared with a negative control. Thus, the authors were able to successfully express biologically active rfrIL-8.
