Electrophoretic Mobility of Cardiac Myosin Heavy Chain Isoforms Revisited: Application of MALDI TOF/TOF Analysis
Autor: | Jitka Zurmanova, Petr L. Jedelsky, Petra Arnostova, Tomáš Soukup |
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Jazyk: | angličtina |
Rok vydání: | 2011 |
Předmět: |
Gene isoform
Male Article Subject lcsh:Biotechnology Health Toxicology and Mutagenesis Blotting Western Molecular Sequence Data lcsh:Medicine Hyperthyroidism Ventricular Myosins Western blot Hypothyroidism lcsh:TP248.13-248.65 Myosin Genetics medicine Animals Protein Isoforms Amino Acid Sequence Molecular Biology Peptide sequence Soleus muscle Heavy chain medicine.diagnostic_test Myosin Heavy Chains Chemistry lcsh:R General Medicine musculoskeletal system Molecular biology Rats Electrophoresis Rats Inbred Lew Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Molecular Medicine Electrophoresis Polyacrylamide Gel Female tissues Sequence Alignment Biotechnology Research Article |
Zdroj: | Journal of Biomedicine and Biotechnology Journal of Biomedicine and Biotechnology, Vol 2011 (2011) |
ISSN: | 1110-7251 1110-7243 |
Popis: | 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 MyHCαwas represented by the lower band with higher mobility and MyHCβby 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 MyHCαpossessed a higher mobility rate than the MyHCβisoform. Our data highlighted the importance of the careful identification of the MyHCαand MyHCβisoforms analyzed by the SDS-PAGE. |
Databáze: | OpenAIRE |
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