Electrophoretic mobility of cardiac myosin heavy chain isoforms revisited: Application of MALDI TOF/TOF analysis

8Citations
Citations of this article
19Readers
Mendeley users who have this article in their library.

This article is free to access.

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 MyHCα was represented by the lower band with higher mobility and MyHCβ 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 MyHCα possessed a higher mobility rate than the MyHCβ isoform. Our data highlighted the importance of the careful identification of the MyHCα and MyHCβ isoforms analyzed by the SDS-PAGE. © 2011 Petra Arnostova et al.

Cite

CITATION STYLE

APA

Arnostova, P., Jedelsky, P. L., Soukup, T., & Zurmanova, J. (2011). Electrophoretic mobility of cardiac myosin heavy chain isoforms revisited: Application of MALDI TOF/TOF analysis. Journal of Biomedicine and Biotechnology, 2011. https://doi.org/10.1155/2011/634253

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free