Abstract
Macrophage migration inhibitory factor (MIF) is a key proinflammatory cytokine. Inhibitors of tautomerase activity of MIF are perspective antiinflammatory compounds. Ceruloplasmin, the copper-containing ferroxidase of blood plasma, is a noncompetitive inhibitor of tautomerase activity of MIF in the reaction with p-hydroxyphenylpyruvate. Small-angle X-ray scattering established a model of the complex formed by MIF and ceruloplasmin. Crystallographic analysis of MIF with a modified active site supports the model. The stoichiometry of 3 CP/MIF trimer complex was established using gel filtration. Conformity of novel data concerning the interaction regions in the studied proteins with previous biochemical data is discussed.
MeSH terms
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Ceruloplasmin / chemistry
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Ceruloplasmin / metabolism*
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Chromatography, Gel
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Copper / chemistry
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Copper / metabolism
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Crystallography, X-Ray
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Fluorescein-5-isothiocyanate / chemistry
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Humans
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Isothiocyanates / chemistry
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Macrophage Migration-Inhibitory Factors / chemistry
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Macrophage Migration-Inhibitory Factors / genetics
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Macrophage Migration-Inhibitory Factors / metabolism*
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Protein Binding
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Protein Structure, Quaternary
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Scattering, Small Angle
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X-Ray Diffraction
Substances
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Isothiocyanates
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Macrophage Migration-Inhibitory Factors
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Recombinant Proteins
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phenylisothiocyanate
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Copper
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Ceruloplasmin
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Fluorescein-5-isothiocyanate