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  • Journal
    Digital Access
    Provider
    Version
    Ovid
    v. 1-47, 1969-2015.
    ScienceDirect
    v. 27-, 1995-
    ClinicalKey
    v. 39-, 2007-
    Print Access Request
    Location
    Version
    Call Number
    Items
    Stored offsite. Please request print.
    v. 11-18, [19], 20-37, 1979-86, [1987], 1988-2005.
    26
  • Article
    Kent C, Vagelos PR.
    Biochim Biophys Acta. 1976 Jun 17;436(2):377-86.
    Plasma membrane from fusing embryonic muscle cells were assayed for phospholipase A activity to determine if this enzyme plays a role in cell fusion. The membranes were assayed under a variety of conditions with phosphatidylcholine as the substrate and no phospholipase A activity was found. The plasma membranes did contain a phosphatidic acid phosphatase which was optimally active in the presence of Triton X-100 and glycerol. The enzyme activity was constant from pH 5.2 to 7.0, and did not require divalent cations. Over 97% of the phosphatidic acid phosphatase activity was in the particulate fraction. The subcellular distribution of the phosphatidic acid phosphatase was the same as the distributions of the plasma membrane markers, (Na+ + k+)-ATPase and the acetylcholine receptor, which indicates that this phosphatase is located exclusively in the plasma membranes. There was no detectable difference in the phosphatidic acid phosphatase activities of plasma membranes from fusing and non-fusing cells.
    Digital Access Access Options