Dimer formation in radiation-irradiated aqueous solution of lysozyme studied by light-scattering-intensity measurement.
The reaction of lysozyme with OH., Br.-2 and e-aq, produced in an aqueous solution by pulsed electrons and gamma-rays, were investigated. Irradiated enzymes showed an increase in the light scattering intensity (LSI) which is proportional to the absorbed dose. Results obtained from SDS gel electrophoresis confirm dimerization of lysozyme, which is considered to be responsible for the increase in LSI. It was found that the rate constant of the dimerization of protein radicals produced in the reaction with OH. is 2K=(1.0 +/- 0.3) X 10(6)M-1 s-1 and the yield of the dimerization is 0.6 in G. The enzymatic activity of the dimer is shown to be reduced to about 30 per cent of that of the intact enzyme. It is concluded that the radiation-induced inactivation of lysozyme is largely due to dimerization.
D004583:Electrons; D005609:Free Radicals; D005720:Gamma Rays; D008027:Light; D008970:Molecular Weight; D009113:Muramidase / Q000528:radiation effects*; D011675:Pulse Radiolysis; D012542:Scattering, Radiation; D014867:Water
D005609:Free Radicals; D014867:Water; D009113:Muramidase