Purification of phospholamban from bovine cardiac muscle with organic solvents
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference20 articles.
1. Phosphorylation of the Sarcoplasmic Reticulum and Sarcolemma
2. Concerted regulation of cardiac sarcoplasmic reticulum calcium transport by cyclic adenosine monophosphate dependent and calcium-calmodulin-dependent phosphorylations
3. Phosphorylation-induced mobility shift in phospholamban in sodium dodecyl sulfate-polyacrylamide gels. Evidence for a protein structure consisting of multiple identical phosphorylatable subunits.
4. Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains.
5. Characterization of structural unit of phospholamban by amino acid sequencing and electrophoretic analysis
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1. Folded State of the Integral Membrane Colicin E1 Immunity Protein in Solvents of Mixed Polarity;Biochemistry;2000-09-15
2. Ion-exchange chromatography of proteins: modulation of selectivity by addition of organic solvents to mobile phase;Journal of Chromatography A;1998-10
3. Phospholamban: Protein Structure, Mechanism of Action, and Role in Cardiac Function;Physiological Reviews;1998-10-01
4. STRUCTURAL PERSPECTIVES OF PHOSPHOLAMBAN, A HELICAL TRANSMEMBRANE PENTAMER;Annual Review of Biophysics and Biomolecular Structure;1997-06
5. Purification of Porcine Phospholamban Expressed inEscherichia coli;Protein Expression and Purification;1996-12
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