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: Purification and properties of phosphoprotein phosphatase from rabbit heart.
    Author: Khandelwal RL.
    Journal: Adv Myocardiol; 1980; 1():345-57. PubMed ID: 6248938.
    Abstract:
    A low molecular weight phosphoprotein phosphatase acting on muscle phosphorylase a has been purified to homogeneity from rabbit heart by acid precipitation, ethanol treatment, and chromatography on Sephadex G-75 and Sepharose-histone. The purified enzyme showed a single band when examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis; the molecular weight calculated by this method was 34,000. The S20,w value and Stockes radius for the enzyme were 3.45 and 24.0 A, respectively. Using these two values, a molecular weight of 35,000 was calculated. Purified enzyme showed a wide substrate specificity and catalyzed the dephosphorylation of phosphorylase a, glycogen synthase D, phosphorylated histone, and phosphorylated casein. A heat-stable protein inhibitor for this enzyme with phosphorylase a as the substrate was also shown to be present in crude extracts of rabbit heart. It inhibited the dephosphorylation of phosphorylase a by phosphoprotein phosphatase by decreasing the Vmax of the reaction.
    [Abstract] [Full Text] [Related] [New Search]