Radiolysis of proteins in the solid state: an approach by EPR and product analysis.
Radio-induced modifications in proteins have been studied using several techniques. Electron paramagnetic resonance (EPR) was used to characterize free radicals, and analysis methods (high-performance liquid chromatography, capillary electrophoresis) were employed to visualize final degraded forms. Whereas EPR indicates that perthiyl radicals are formed, analysis does not detect any compound in which such bonds would be broken. Since EPR signals decay with time, it is concluded that rearrangements occur at subsequent steps, in which the solvent used during the analysis might play a role.
Terryn
Hélène
H
Université Catholique de Louvain, Faculté de Médecine, Département de Pharmacie, Unité CHAM 72.30, Bruxelles, Belgium.
Deridder
Véronique
V
Sicard-Roselli
Cécile
C
Tilquin
Bernard
B
Houée-Levin
Chantal
C
D000818:Animals; D002645:Chickens; D002851:Chromatography, High Pressure Liquid; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D004586:Electrophoresis; D006801:Humans; D007328:Insulin / Q000737:chemistry* / Q000528:radiation effects*; D009113:Muramidase / Q000737:chemistry* / Q000528:radiation effects; D011487:Protein Conformation / Q000528:radiation effects; D011675:Pulse Radiolysis / Q000379:methods*; D013696:Temperature
D007328:Insulin; D009113:Muramidase