echemi logo
Product
  • Product
  • Supplier
  • Inquiry
    Home > Biochemistry News > Biotechnology News > Measurement of S-Glutathionated Hemoglobin in Human Erythrocytes by Isoelectric Focusing Electrophoresis

    Measurement of S-Glutathionated Hemoglobin in Human Erythrocytes by Isoelectric Focusing Electrophoresis

    • Last Update: 2021-03-06
    • Source: Internet
    • Author: User
    Search more information of high quality chemicals, good prices and reliable suppliers, visit www.echemi.com
    Protein thiol groups are susceptible to oxidation by reactive oxygen species (
    1
    ). The occurrence of a specific thiol modification named protein S-glutathionation has been proposed to protect proteins from oxidative damage owing to its reversible characteristics (
    2

    4
    ). In addition, S-glutathionation modulates protein functions including enzyme activity (
    4

    5
    ), cytoskeletal protein strength (
    6
    ), hemoglobin-gelling activity (
    7
    ), and chaperon activity (
    8
    ). Because an increase in cellular glutathione (GSSG) level is correlated with the formation of S-glutathionated protein, a mixed-disulfide exchange reaction has been proposed to be responsible for this protein modification (
    2

    5
    ,
    9

    10
    ). However, glutathione (GSH) modified proteins are also formed under a circumstance without significant change in GSSG level (
    11

    12
    ), and a radical-initiated process has therefore also been proposed (
    3
    ). S-Gluthionated hemoglobin formation owing to oxidative stress has been noted in the red blood cells from different species (
    13

    15
    ). There are a total of six cysteine residues in the human hemoglobin molecule, but two of them (β93 residues) are highly reactive (
    16
    ) and can form mixed disulfide with GSH (
    14
    ). However, the location of reactive cysteines in hemoglobin varies in different animal species. For example, the cysteines in chicken α-hemoglobin are more active than those in β hemoglobin (
    15
    ).
    This article is an English version of an article which is originally in the Chinese language on echemi.com and is provided for information purposes only. This website makes no representation or warranty of any kind, either expressed or implied, as to the accuracy, completeness ownership or reliability of the article or any translations thereof. If you have any concerns or complaints relating to the article, please send an email, providing a detailed description of the concern or complaint, to service@echemi.com. A staff member will contact you within 5 working days. Once verified, infringing content will be removed immediately.

    Contact Us

    The source of this page with content of products and services is from Internet, which doesn't represent ECHEMI's opinion. If you have any queries, please write to service@echemi.com. It will be replied within 5 days.

    Moreover, if you find any instances of plagiarism from the page, please send email to service@echemi.com with relevant evidence.