Today's Hours: 8:00am - 10:00pm
Lane Medical Library

Search

Filter Results

Did You Mean:

Search Results

Sort by
relevance
  • Book
    Digital Access ScienceDirect v. 1-17, 1996-2005.
    Print
    Location
    Version
    Call Number
    Items
    Books: General Collection (Downstairs)
    v. 5-6, 8-9, 17, 2001-02, 2005.
    Call number varies. Search for Advances in cell aging and gerontology to find individual volumes of this title.
  • Article
    Boonman JC, van Beek GG, Muijsers AO, van Gelder BF.
    Mol Cell Biochem. 1979 Aug 15;26(3):183-92.
    About 45% of the protein can be removed from oxidized cytochrome c oxidase by treatment with proteolytic enzymes under a variety of conditions, leading to an increased heme to protein ratio. The principal spectroscopic parameters of cytochrome c oxidase are retained in the protease-treated enzyme. Of the overall catalytic activity 20% remained after digestion; the electron-transfer reactions were impaired but the affinity for cytochrome c appeared unchanged. Proteolysis resulted in removal of the hydrophobic subunit III and most of the smaller hydrophilic subunits, leaving a core, which basically consists of the two largest subunits I and II. The subunits I and/or II carry the prosthetic groups of the enzyme and at least one of the cytochrome c binding sites. The smaller subunits, however, are essential for optimal electron transfer and possibly have other functions as well.
    Digital Access Access Options