Purification of phospholamban from bovine cardiac muscle with organic solvents

P. Boyot, B. Luu, Larry Jones, E. Trifilieff

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Phospholamban (PLB), an integral membrane protein of cardiac sarcoplasmic reticulum, was extracted from bovine cardiac muscle with an acidic chloroform/methanol mixture. A combination of gel permeation and ion-exchange chromatographies in organic solvents allowed the purification of PLB. The intensive use of organic solvents throughout the isolation yielded a highly purified and intact protein that can be phosphorylated by cAMP protein kinase. The ease of purification and the high yield obtained (2.5 mg/100 g of fresh tissue) show that organic solvents can be very useful in the extraction and purification of hydrophobic membrane proteins.

Original languageEnglish
Pages (from-to)639-645
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume269
Issue number2
DOIs
StatePublished - 1989

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Organic solvents
Purification
Muscle
Myocardium
Membrane Proteins
Ion Exchange Chromatography
Sarcoplasmic Reticulum
Chloroform
Chromatography
Permeation
Protein Kinases
Methanol
Ion exchange
Gels
Tissue
phospholamban
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Purification of phospholamban from bovine cardiac muscle with organic solvents. / Boyot, P.; Luu, B.; Jones, Larry; Trifilieff, E.

In: Archives of Biochemistry and Biophysics, Vol. 269, No. 2, 1989, p. 639-645.

Research output: Contribution to journalArticle

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