Determination of the monomer-dimer equilibrium of interleukin-8 reveals it is a monomer at physiological concentrations
Biochemistry1994Vol. 33(43), pp. 12741–12745
Citations Over TimeTop 10% of 1994 papers
Sally Burrows, Michael L. Doyle, Kenneth P. Murphy, Samuel G. Franklin, John R. White, Ian Brooks, Dean E. McNulty, Miller O. Scott, Jay R. Knutson, Denise Porter, Peter R. Young, Preston Hensley
Abstract
Interleukin-8 has been shown by X-ray crystallography and NMR to be a homodimer, suggesting that this is the form which binds to its receptor. Here we measure, for the first time, the monomer-dimer equilibrium of interleukin-8 using analytical ultracentrifugation and titration microcalorimetry and find that it dissociates readily to monomers with an equilibrium dissociation constant of 18 +/- 6 microM at 37 degrees C. The present findings suggest that the monomer is the form which binds to the receptor. Comparison of experimental and structure-based calculated thermodynamics of interleukin-8 dimerization argues for limited subunit conformational changes upon dissociation to monomer.
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