Mass spectrometry analyses of rat 2b myosin heavy chain isoform
Language English Country Czech Republic Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
17973598
DOI
10.33549/physiolres.931280
PII: 1280
Knihovny.cz E-resources
- MeSH
- Chromatography, Liquid MeSH
- Databases, Protein MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Spectrometry, Mass, Electrospray Ionization * MeSH
- Protein Conformation MeSH
- Muscle, Skeletal chemistry MeSH
- Rats MeSH
- Molecular Sequence Data MeSH
- Nonmuscle Myosin Type IIB chemistry isolation & purification MeSH
- Peptide Mapping MeSH
- Amino Acid Sequence MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization * MeSH
- Tandem Mass Spectrometry * MeSH
- Myosin Heavy Chains chemistry isolation & purification MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Nonmuscle Myosin Type IIB MeSH
- nonmuscle myosin type IIB heavy chain MeSH Browser
- Myosin Heavy Chains MeSH
We have separated 2b myosin heavy chain (MyHC) isoform from the rat extensor digitorum longus muscle by SDS-PAGE and analyzed it by two subsequent mass spectrometry techniques. After tryptic digestion, the obtained peptides were identified by Matrix-Assisted Laser Desorption/Ionisation reflectron Time of Flight mass spectrometry (MALDI-TOF MS) and sequenced by liquid chromatography tandem mass spectrometry (ESI LC/MS/MS). The analyzed peptides proportionally covered 30 % of the 2b MyHC isoform sequence. The results suggest that the primary structure is identical with the highest probability to a NCBI database record ref|NP_062198.1|, representing the last updated record of rat 2b isoform. Nonetheless, four peptides carrying amino acid substitution(s) in comparison with the NCBI database record were identified.
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