Purification of thiol:protein-disulfide oxidoreductase from bovine liver
DOI: 10.1016/0003-2697(84)90490-1
Title: Purification of thiol:protein-disulfide oxidoreductase from bovine liver
Journal Title: Analytical Biochemistry
Volume: 142
Issue: 2
Publication Date: 1 November 1984
Start Page: 463
End Page: 466
Published online: online 6 December 2004
ISSN: 0003-2697
Author: Svein Bjelland, Bent Foltmann, Knut Wallevik
Affiliations:

  • The Finsen Laboratory, The Finsen Institute, 49 Strandboulevarden, DK 2100 Copenhagen Ø, Denmark

  • Institute of Biochemical Genetics, University of Copenhagen, 2A Øster Farimagsgade, DK 1353 Copenhagen K, Denmark
  • Abstract: Purification procedure of thiol:protein-disulfide oxidoreductase (EC 1.8.4.2) from bovine liver has been developed. The procedure is based on that of D. F. Carmichael, J. E. Morin, and J. E. Dixon (1977, J. Biol. Chem.252, 7163–7167), and contains the following steps: homogenization in Triton X-100, selective heat denaturation, chromatography on CM-Sephadex C-50, and chromatography on DEAE-Sephadex A-50. The final preparation has a high specific activity and a high level of purity as judged by sodium dodecyl sulfatepolyacrylamide gel electrophoresis.
    Received: 15 February 1984
    Keywords: disulfide bonds; protein-disulfide interchange; thiol; protein-disulfide oxidoreductase; glutathione-insulin transhydrogenase; protein-disulfide isomerase; disulfide interchange enzyme

    Please Share this Paper with friends:
    Comment
    No.
    Comment Content
    User Name
    Date
    Post new Comment
    UserName
    Post to Facebook
    ×
    Search Full Text