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Article
Study of Calsequestrin Aggregation by Flow Field‐Flow Fractionation with Light Scattering Detection
Journal of Liquid Chromatography & Related Technologies
  • Susan Shadle, Boise State University
  • Randy Rostock, Boise State University
  • Lou Bonfrisco, Boise State University
  • Martin Schimpf, Boise State University
Document Type
Article
Publication Date
1-2-2007
Disciplines
Abstract
Flow field-flow fractionation with multi-angle light scattering detection indicates that calsequestrin forms even-numbered aggregates, supporting the view that this Ca2+ binding protein aggregates through the interaction of dimers. Contrary to previous reports based on size exclusion chromatography FlFFF further indicates that the dimer is the stable species, with very little monomer present under the conditions analyzed in this study. Increasing the concentration of K+ (100-700 mM) causes the dimer to be the increasingly dominant species over monomer, tetramer, and other aggregate species. Increasing the concentration of Ca2+ (3-10 mM) causes increased aggregation of dimers into higher order species. Finally, addition of small amounts of the anthracycline analog trifluoperazine (0.10–0.50 mM), which is known to disrupt calsequestrin function, induces severe aggregation.
Citation Information
Susan Shadle, Randy Rostock, Lou Bonfrisco and Martin Schimpf. "Study of Calsequestrin Aggregation by Flow Field‐Flow Fractionation with Light Scattering Detection" Journal of Liquid Chromatography & Related Technologies (2007)
Available at: http://works.bepress.com/martin_schimpf/14/