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Updated: May 4, 2026
Matrix-assisted Laser Desorption/Ionization Time of Flight MALDI-TOF Mass Spectrometric Analysis of Intact Proteins Larger than 100 kDa
Published on: September 9, 2013
LC MS/MS identification of large structural proteins from bull muscle and their degradation products during post
Guojie Wu1, Stefan Clerens2, Mustafa M Farouk1
1AgResearch, Ruakura Research Centre, Hamilton, New Zealand.
Abstract:
Large proteins (>100kDa) in bovine M. longissimus dorsi and their degradation products during post mortem ageing were investigated by gel electrophoresis and LC-MS/MS analysis. Seventeen protein bands from SDS-PAGE were analysed and 26 proteins were identified. Intact titin, nebulin and filamin were shown to break down during post mortem ageing of meat. A number of myosin super-family members were revealed on SDS-PAGE. Myosin heavy chain 1 (MYH1), myosin heavy chain 2 (MYH2), and myosin heavy chain 7 (MYH7) were distributed broadly across the bands in the forms of cross-linked/aggregated polymers, and also as fragments. Three myomesin family members: myomesin 1 (185kDa isoform 1), myomesin (M-protein) 2, 165kDa, and myomesin family member 3, were identified in the muscle samples. Several other proteins such as synemin, myosin binding protein C (C-protein), glycogen debranching enzyme and ryanodine receptor 2 were also identified.
