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: Phospholamban stoichiometry in canine cardiac muscle sarcoplasmic reticulum.
    Author: Louis CF, Turnquist J, Jarvis B.
    Journal: Neurochem Res; 1987 Oct; 12(10):937-41. PubMed ID: 2960909.
    Abstract:
    Treatment of cardiac sarcoplasmic reticulum with the crosslinking reagent dithiobis (succinimidyl propionate) in the presence of 125I-calmodulin, resulted in the formation of a 40,000-dalton affinity labeled component, consisting of a 1:1, phospholamban: 125I-calmodulin complex. In parallel experiments, sarcoplasmic reticulum was phosphorylated in the presence of calmodulin and [gamma-32P]ATP, and then treated with the crosslinking reagent to produce an affinity labeled component consisting of a 1:1, calmodulin: 32P-phospholamban complex. These experiments permitted determination of the amount of 125I and 32P incorporated into the 40,000-dalton complexes, as well as the amount of 32P incorporated into the 23,000-dalton form of phospholamban. If 1 mol of Ca2+-dependent ATPase phosphoprotein represents 1 mol of 100,000-dalton Ca2+-dependent ATPase monomer, then there are 4.88 +/- 1.33 mol Ca2+-dependent ATPase/mol of phospholamban. If there are 2 mol of Ca2+-dependent ATPase phosphoprotein/mol of 100,000-dalton Ca2+-dependent ATPase monomer, then there are 9.76 +/- 2.66 mol Ca2+-dependent ATPase/mol phospholamban.
    [Abstract] [Full Text] [Related] [New Search]