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Related Experiment Videos

Zn2+ binding to cardiac calsequestrin

S Baksh1, C Spamer, K Oikawa

  • 1Department of Pediatrics, University of Alberta, Edmonton, Canada.

Biochemical and Biophysical Research Communications
|April 6, 1995
PubMed
Summary
This summary is machine-generated.

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Cardiac calsequestrin binds significant amounts of zinc (Zn2+), potentially modulating its structure and function. This study confirms calsequestrin as a dual calcium and zinc-binding protein.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cardiology

Background:

  • Cardiac calsequestrin is crucial for calcium (Ca2+) handling in heart muscle.
  • The role of other divalent cations, like zinc (Zn2+), in calsequestrin function is less understood.

Purpose of the Study:

  • To investigate the binding of zinc (Zn2+) to canine cardiac calsequestrin.
  • To determine the affinity and characteristics of Zn2+ interaction with calsequestrin.

Main Methods:

  • Utilized Zn2+-specific fluorescence dye salicylcarbohydrazone (SACH).
  • Employed 65Zn2+ overlay assays and Zn(2+)-IDA chromatography.
  • Analyzed protein conformation using circular dichroism.

Main Results:

Related Experiment Videos

  • Cardiac calsequestrin binds approximately 200 moles of Zn2+ per mole of protein (Kd = 300 microM).
  • Zn2+ binding induced protein aggregation but did not involve histidine residues.
  • Observed only minor Zn2+-dependent conformational changes via circular dichroism.

    • Conclusions:

    • Cardiac calsequestrin is a Ca2+- and Zn2+-binding protein.
    • Zn2+ binding may influence calsequestrin's structure and function in cardiac muscle.