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Publication Detail
Proteomic analysis of UVC irradiation-induced damage of plasma proteins: Serum amyloid P component as a major target of photolysis
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Article
  • Authors:
    Chan HL, Gaffney PR, Waterfield MD, Anderle H, Peter MH, Schwarz HP, Turecek PL, Timms JF
  • Publication date:
    29/05/2006
  • Pagination:
    3229, 3236
  • Journal:
    FEBS LETT
  • Volume:
    580
  • Issue:
    13
  • Print ISSN:
    0014-5793
  • Keywords:
    analysis, blood, Blood Proteins, CANCER, Disinfection, Humans, London, Mass, methods, Oxidative Stress, Photolysis, Proteomics, radiation effects, Research Support, Non-U.S.Gov't, Serum Amyloid P-Component, Spectrum Analysis, Mass, STRATEGIES, Sulfhydryl Compounds, Ultraviolet Rays
  • Addresses:
    Ludwig Institute for Cancer Research and Department of Biochemistry and Molecular Biology, University College London, Cruciform Building, Gower Street, London WC1E 6BT, UK
  • Notes:
    DA - 20060524ISSN: - 0014-5793 (Print)LA - engPT - Journal ArticleRN - 0 (Blood Proteins)RN - 0 (Serum Amyloid P-Component)RN - 0 (Sulfhydryl Compounds)SB - IM
Abstract
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
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