Dissociation equilibrium of human recombinant interferon gamma

Biochemistry
R BotevaB Salvato

Abstract

The biologically active form of interferon gamma is a dimer composed of two noncovalently bound identical polypeptide chains of 17 kDa each. In this study, it was found that dissociation of the dimer into monomers significantly reduced the fluorescence quantum yield and the efficiency of the intermolecular Tyr to Trp radiationless energy transfer. The same process caused significant changes in the fluorescence decay and in the fluorescence anisotropy decay. The kinetic and thermodynamic parameters of the dimer-monomer equilibrium were determined by fluorescence measurements at different temperatures and by a theoretical mathematical model. Dissociation of the dimers into monomers was an endothermic process and was favored by concentrations of the protein lower than 1 microM and by increasing the temperature. It was accompanied by formation of aggregates, a slow and partially reversible process leading to inactivation of the interferon. It is suggested that certain monomeric conformers are competent for aggregation.

References

Jan 1, 1987·Annual Review of Biochemistry·S PestkaC E Samuel
Feb 1, 1981·Journal of Virology·S RubinsteinS Pestka

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Citations

Mar 26, 1998·International Journal of Biological Macromolecules·P K Nandi
Jan 11, 2000·International Journal of Biological Macromolecules·T ZlatevaR Tsanev
Apr 16, 2005·Drug Development and Industrial Pharmacy·Sara SeguraJuan Manuel Irache
Mar 10, 2016·Protein Engineering, Design & Selection : PEDS·Gaurav GhagVijayaraghavan Rangachari
May 9, 2015·Food Chemistry·Jelena VesicTanja Cirkovic Velickovic
Apr 2, 2014·Journal of Immunological Methods·Chen ShenGottfried Koehler
Jul 31, 2020·The Journal of Immunology : Official Journal of the American Association of Immunologists·Sergey A TarasovOleg I Epstein
Dec 1, 2020·Proteins·Anukool A Bhopatkar, Vijayaraghavan Rangachari
Oct 24, 2000·Journal of Pharmaceutical Sciences·M L van SlootenW Jiskoot

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