Curtin University Homepage
  • Library
  • Help
    • Admin

    espace - Curtin’s institutional repository

    JavaScript is disabled for your browser. Some features of this site may not work without it.
    View Item 
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item

    Quantitative determination of polysulfide in albumins, plasma proteins and biological fluid samples using a novel combined assays approach

    Access Status
    Fulltext not available
    Authors
    Ikeda, M.
    Ishima, Y.
    Shibata, A.
    Chuang, Victor
    Sawa, T.
    Ihara, H.
    Watanabe, H.
    Xian, M.
    Ouchi, Y.
    Shimizu, T.
    Ando, H.
    Ukawa, M.
    Ishida, T.
    Akaike, T.
    Otagiri, M.
    Maruyama, T.
    Date
    2017
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Ikeda, M. and Ishima, Y. and Shibata, A. and Chuang, V. and Sawa, T. and Ihara, H. and Watanabe, H. et al. 2017. Quantitative determination of polysulfide in albumins, plasma proteins and biological fluid samples using a novel combined assays approach. Analytica Chimica Acta. 969: pp. 18-25.
    Source Title
    Analytica Chimica Acta
    DOI
    10.1016/j.aca.2017.03.027
    ISSN
    0003-2670
    School
    School of Pharmacy
    URI
    http://hdl.handle.net/20.500.11937/53344
    Collection
    • Curtin Research Publications
    Abstract

    Hydrogen sulfide (H2S) signaling involves polysulfide (RSSnSR') formation on various proteins. However, the current lack of sensitive polysulfide detection assays poses methodological challenges for understanding sulfane sulfur homeostasis and signaling. We developed a novel combined assay by modifying Sulfide Antioxidant Buffer (SAOB) to produce an “Elimination Method of Sulfide from Polysulfide” (EMSP) treatment solution that liberates sulfide, followed with methylene blue (MB) sulfide detection assay. The combined EMSP-MB sulfide detection assay performed on low molecular weight sulfur species showed that sulfide was produced from trisulfide compounds such as glutathione trisulfide and diallyl trisulfide, but not from the thiol compounds such as cysteine, cystine and glutathione. In the case of plasma proteins, this novel combined detection assay revealed that approximately 14.7, 1.7, 3.9, 3.7 sulfide mol/mol released from human serum albumin, a1-anti-trypsin, a1-acid glycoprotein and ovalbumin, respectively, suggesting that serum albumin is a major pool of polysulfide in human blood circulation. Taken together with the results of albumins of different species, the liberated sulfide has a good correlation with cysteine instead of methionine, indicating the site of incorporation of polysulfide is cysteine. With this novel sulfide detention assay, approximately 8,000, 120 and 1100 µM of polysulfide concentrations was quantitated in human healthy plasma, saliva and tear, respectively. Our promising polysulfide specific detection assay can be a very important tool because quantitative determination of polysulfide sheds light on the functional consequence of protein-bound cysteine polysulfide and expands the research area of reactive oxygen to reactive polysulfide species.

    Related items

    Showing items related by title, author, creator and subject.

    • Malodorous dimethylpolysulfides in Perth drinking water.
      Heitz, Anna (2002)
      The formation of an objectionable "swampy" odour in drinking water distribution systems in Perth, Western Australia, was first described by Wajon and co-authors in the mid-1980s (Wajon et al., 1985; Wajon et al., 1986; ...
    • Analysis of polysulfides in drinking water distribution systems using headspace solid-phase microextraction and gas chromatography-mass spectrometry
      Kristiana, Ina; Heitz, Anna; Joll, Cynthia; Sathasivan, Arumugam (2010)
      Sulfide and polysulfides are strong nucleophiles and reducing agents that participate in many environmentally significant processes such as the formation of sulfide minerals and volatile organic sulfur compounds. Their ...
    • Human serum albumin hydropersulfide is a potent reactive oxygen species scavenger in oxidative stress conditions such as chronic kidney disease
      Shibata, A.; Ishima, Y.; Ikeda, M.; Sato, H.; Imafuku, T.; Chuang, Victor; Ouchi, Y.; Abe, T.; Watanabe, H.; Ishida, T.; Otagiri, M.; Maruyama, T. (2016)
      Recently, hydropersulfide (RSSH) was found to exist in mammalian tissues and fluids. Cysteine hydropersulfide can be found in free cysteine residues as well as in proteins, and it has potent antioxidative activity. Human ...
    Advanced search

    Browse

    Communities & CollectionsIssue DateAuthorTitleSubjectDocument TypeThis CollectionIssue DateAuthorTitleSubjectDocument Type

    My Account

    Admin

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Follow Curtin

    • 
    • 
    • 
    • 
    • 

    CRICOS Provider Code: 00301JABN: 99 143 842 569TEQSA: PRV12158

    Copyright | Disclaimer | Privacy statement | Accessibility

    Curtin would like to pay respect to the Aboriginal and Torres Strait Islander members of our community by acknowledging the traditional owners of the land on which the Perth campus is located, the Whadjuk people of the Nyungar Nation; and on our Kalgoorlie campus, the Wongutha people of the North-Eastern Goldfields.