These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Identification of inhibitor-2 as the ATP-mg-dependent protein phosphatase modulator.
    Author: Yang SD, Vandenheede JR, Merlevede W.
    Journal: J Biol Chem; 1981 Oct 25; 256(20):10231-4. PubMed ID: 6270104.
    Abstract:
    In previous reports (Yang, S. D., Vandenheede, J. R., Goris, J., and Merlevede, W. (1980) J. Biol. Chem. 255, 11759-11767; Vandenheede, J. R., Yang, S.-D., and Merlevede, W. (1981) J. Biol. Chem. 256, 5894-5900), we have described two slightly different purification procedures for the isolation of the inactive ATP-Mg-dependent protein phosphatase (FC) which could be activated by a protein activator (FA) in the presence of ATP-Mg. Although the two procedures consistently produced FC preparations that showed very similar polyacrylamide gel patterns, the specific activity of the purified enzymes varied considerably. The preparations characterized by a rather low specific activity could be stimulated up to 10-fold when a titrated amount of inhibitor-2 was included during the FA and ATP-Mg-mediated activation. Inhibitor-2, only recently implicated as an inactivating protein for activated FC (Vandenheede, J. R., Goris, J., Yang, S.-D., Camps, T., and Merlevede, W. (1981) FEBS Lett. 127, 1-3) has now been identified as a modulator protein, necessary for the reversible activation of the protein phosphatase.
    [Abstract] [Full Text] [Related] [New Search]