Comparison of new ELISA method with established SDS-PAGE method for determination of muscle myosin heavy chain isoforms
Language English Country Czech Republic Media print-electronic
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
PubMed
21995898
DOI
10.33549/physiolres.932213
PII: 932213
Knihovny.cz E-resources
- MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Enzyme-Linked Immunosorbent Assay MeSH
- Rats, Inbred Strains MeSH
- Rats MeSH
- Rats, Inbred Lew MeSH
- Protein Isoforms analysis MeSH
- Muscle Fibers, Slow-Twitch chemistry physiology MeSH
- Muscle Fibers, Fast-Twitch chemistry physiology MeSH
- Myosin Heavy Chains analysis MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Female MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Protein Isoforms MeSH
- Myosin Heavy Chains MeSH
We developed a new method for the quantitative determination of myosin heavy chain (MyHC) isoforms taking advantage of immunochemical differences and based on the ELISA principle. In the present paper we compare analysis of MyHC isoforms using the SDS-PAGE and the ELISA methods in the same samples of adult female inbred Lewis strain euthyroid, hyperthyroid and hypothyroid rats. In all thyroid states, the same composition and corresponding changes of MyHC isoforms were determined using both methodological approaches in the slow soleus and the fast extensor digitorum longus muscles. Our results showed that ELISA can be used for a "semi-quantitative" or "comparative" measurement of MyHC isoforms in multiple muscle samples, but that it is neither more exact nor faster compared to SDS-PAGE.
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