Open AccessMass spectroscopy analyses of rat 2b myosin heavy chain isoform
Author(s) -
Jitka Žurmanová,
Daniela Malacova,
František Půta,
Petr Novák,
Jan Říčný,
Tomáš Soukup
Publication year - 2007
Publication title -
physiological research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.647
H-Index - 70
eISSN - 1802-9973
pISSN - 0862-8408
DOI - 10.33549/physiolres.931280
Subject(s) - myosin , gene isoform , chemistry , mass spectrometry , tandem mass spectrometry , protein primary structure , protein mass spectrometry , peptide , chromatography , peptide sequence , biochemistry , gene
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.