LC MS/MS identification of large structural proteins from bull muscle and their degradation products during post mortem storage

Food Chem. 2014 May 1:150:137-44. doi: 10.1016/j.foodchem.2013.10.158. Epub 2013 Nov 2.

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.

Keywords: LC–MS/MS; Muscle structural proteins; Myosin super-family; Post mortem storage; Protein identification; SDS–PAGE.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Chromatography, Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Meat / analysis*
  • Molecular Weight
  • Muscle Proteins / chemistry*
  • Muscle, Skeletal / chemistry*
  • Postmortem Changes
  • Protein Conformation
  • Tandem Mass Spectrometry / methods

Substances

  • Muscle Proteins