A simplified method for identification of human cardiac myosin heavy-chain isoforms

Shengfu Piao, Fushun Yu, Michael J. Mihm, Peter J. Reiser, Patrick M. McCarthy, David R. Van Wagoner, John Anthony Bauer*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


Cardiac myosin is a central participant in the crossbridge cycling that mediates myocyte contraction and consists of multiple subunits that mediate both hydrolysis of ATP and mechanical production of contractile force Two isoforms of myosin heavy chain (MHC-α and MHC-β) are known to exist in mammalian cardiac tissue, and it is within this myosin subunit that ATPase activity resides. These isoforms differ by less than 0.2% in total molecular mass and amino acid sequence, but, strikingly, influence the rate and efficiency of energy utilization for generation of contractile force. Changes in the MHC-α/MHC-β ratio has been classically viewed as an adaptation of a failing myocyte in both animal models and humans; however, their measurement has traditionally required specialized preparations and materials for sufficient resolution. Here we describe a greatly simplified method for routine assessments of myosin isoform composition in human cardiac tissues. The primary advantages of our approach include higher throughput and reduced supply costs with no apparent loss of statistical power, reproducibility or achieved results. Use of this more convenient method may provide enhanced access to an otherwise specialized technique and could provide additional opportunity for investigation of cardiac myocyte adaptive changes.

Original languageEnglish (US)
Pages (from-to)27-30
Number of pages4
JournalBiotechnology and Applied Biochemistry
Issue number1
StatePublished - Feb 2003


  • Atrial fibrillation
  • Electrophoresis
  • Heart failure

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Molecular Medicine
  • Biomedical Engineering
  • Applied Microbiology and Biotechnology
  • Drug Discovery
  • Process Chemistry and Technology


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