Related Experiment Videos
Neutrophil activation by monomeric interleukin-8
K Rajarathnam1, B D Sykes, C M Kay
1Protein Engineering Network of Centres of Excellence (PENCE), University of Alberta, Edmonton, Canada.
Science (New York, N.Y.)
|April 1, 1994
Abstract:
Interleukin-8 (IL-8), a pro-inflammatory protein, has been shown by nuclear magnetic resonance (NMR) and x-ray techniques to exist as a homodimer. An IL-8 analog was chemically synthesized, with the amide nitrogen of leucine-25 methylated to selectivity block formation of hydrogen bonds between monomers and thereby prevent dimerization. This analog was shown to be a monomer, as assessed by analytical ultracentrifugation and NMR. Nevertheless, it was equivalent to IL-8 in assays of neutrophil activation, which indicates that the monomer is a functional form of IL-8.