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Proteomic analysis of UVC irradiation‐induced damage of plasma proteins: Serum amyloid P component as a major target of photolysis
Author(s) -
Chan Hong-Lin,
Gaffney Piers R.,
Waterfield Michael D.,
Anderle Heinz,
Peter Matthiessen H.,
Schwarz Hans-Peter,
Turecek Peter L.,
Timms John F.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.05.002
Subject(s) - chemistry , photodissociation , serum amyloid p component , thiol , reactivity (psychology) , mass spectrometry , blood proteins , fluorescence , irradiation , protein carbonylation , protein aggregation , photochemistry , biochemistry , biophysics , oxidative stress , chromatography , oxidative damage , c reactive protein , biology , immunology , medicine , physics , alternative medicine , pathology , quantum mechanics , nuclear physics , inflammation
Ultraviolet‐C (UVC) irradiation is a pathogen inactivation method used for disinfection of pharmaceutical products derived from human blood. Previous studies have shown that UVC can potentially damage proteins through photolysis or can generate reactive species resulting in protein thiol oxidation. In this study, two fluorescence‐based quantitative proteomic approaches were used to assess the effects of a novel UVC‐disinfection strategy on human plasma fractions. We show minimal changes in protein content, but gross alterations in protein thiol reactivity, indicative of oxidative damage. We identify a number of the damaged proteins by mass spectrometry, including serum amyloid P component, and further demonstrate UVC‐induced photolysis of its disulphide bond.