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Journal of Biomedicine and Biotechnology
Volume 2011 (2011), Article ID 634253, 9 pages
http://dx.doi.org/10.1155/2011/634253
Research Article

Electrophoretic Mobility of Cardiac Myosin Heavy Chain Isoforms Revisited: Application of MALDI TOF/TOF Analysis

1Department of Physiology, Faculty of Science, Charles University in Prague, 12843 Prague, Czech Republic
2Department of Cell Biology, Faculty of Science, Charles University in Prague, 12843 Prague, Czech Republic
3Department of Parasitology, Faculty of Science, Charles University in Prague, 12843 Prague, Czech Republic
4Laboratory of Mass Spectrometry, Faculty of Science, Charles University in Prague, 12843 Prague, Czech Republic
5Institute of Physiology, Academy of Sciences of the Czech Republic, v.v.i., 14220 Prague, Czech Republic

Received 24 June 2011; Accepted 9 September 2011

Academic Editor: Henk Granzier

Copyright © 2011 Petra Arnostova et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

The expression of two cardiac myosin heavy chain (MyHC) isoforms in response to the thyroid status was studied in left ventricles (LVs) of Lewis rats. Major MyHC isoform in euthyroid and hyperthyroid LVs had a higher mobility on SDS-PAGE, whereas hypothyroid LVs predominantly contained a MyHC isoform with a lower mobility corresponding to that of the control soleus muscle. By comparing the MyHC profiles obtained under altered thyroid states together with the control soleus, we concluded that MyHC was represented by the lower band with higher mobility and MyHC by the upper band. The identity of these two bands in SDS-PAGE gels was confirmed by western blot and mass spectrometry. Thus, in contrast to the literature data, we found that the MyHC possessed a higher mobility rate than the MyHC isoform. Our data highlighted the importance of the careful identification of the MyHC and MyHC isoforms analyzed by the SDS-PAGE.