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March 1, 1985Journal of Biological ChemistryOpen Access

Purification and characterization of phospholamban from canine cardiac sarcoplasmic reticulum.

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Population

Canine cardiac sarcoplasmic reticulum (SR) membranes

Design

Preclinical

Authors

MIMasayuki InuiResearch Institute of Innovative Technology for the EarthMKMasaaki KadomaThe University of OsakaMTMichihiko TadaUniversity of Vermont

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Implication

Supports biochemical dissection of cardiac SR regulation in models; leaves open human therapeutic translation.

Key Points

  • The study aims to purify and characterize phospholamban to understand its role as a regulator of calcium transport in cardiac sarcoplasmic reticulum.
  • Phospholamban was purified from canine cardiac SR using deoxycholate extraction and ammonium sulfate fractionation.
  • Further purification involved gel permeation high performance liquid chromatography and CM-Sepharose CL 6B column chromatography with nonionic detergent C12E8.
  • Antisera were prepared against purified phospholamban to facilitate binding studies.
  • Purified phospholamban showed a molecular weight of 22,000 daltons on SDS-PAGE.
  • Phosphorylation increased its weight slightly to 27,000 daltons, with a phosphorylation extent of 42 nmol of phosphate/mg of protein.
  • Antisera bound specifically to phospholamban in cardiac SR but did not react with fast skeletal muscle SR.

Structured PICO

P
Population
Canine cardiac sarcoplasmic reticulum (SR) membranes
I
Intervention
Purification and characterization of phospholamban
O
Outcome
Molecular weight, phosphorylation extent, and antibody binding of purified phospholambansurrogate

The purification and characterization of phospholamban from canine cardiac sarcoplasmic reticulum provides a foundation for understanding its regulatory action on the calcium pump ATPase.

Cite This Study

Inui et al. (1985) studied this question.

synapsesocial.com/papers/6a720ca75d37378ac1defc14https://doi.org/10.1016/s0021-9258(19)83681-5
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Purification of phospholamban, a 22,000-dalton protein from cardiac sarcoplasmic reticulum that is specifically phosphorylated by cyclic AMP-dependent protein kinase.1982 · 37 citations
  2. 2Phospholamban, activator of the cardiac sarcoplasmic reticulum calcium pump. Physicochemical properties and diagonal purification1980 · 79 citations
  3. 3Effects of adenosine 3':5'-monophosphate-dependent protein kinase on sarcoplasmic reticulum isolated from cardiac and slow and fast contracting skeletal muscles.1976 · 191 citations
  4. 4Cholinergic antagonism of beta-adrenergic stimulation of cardiac membrane protein phosphorylation in situ.1983 · 39 citations
  5. 5Concerted regulation of cardiac sarcoplasmic reticulum calcium transport by cyclic adenosine monophosphate dependent and calcium-calmodulin-dependent phosphorylations1979 · 456 citations