Adaptation of two-dimensional electrophoresis for muscle tissue analysis


  • Anastasiya Akhremko V. M. Gorbatov Federal Research Center for Food Systems of RAS, Experimental-clinical research laboratory of bioactive substances of animal origin, Talalikhina st., 26, 109316, Moscow, Russia, Tel.: +79152379497
  • Ekaterina Romanovna Vasilevskaya V. M. Gorbatov, Federal Research Center for Food Systems of RAS, Experimental-clinical research laboratory of bioactive substances of animal origin, Talalikhina st., 26, 109316, Moscow, Russia, Tel.: +79688223598
  • Liliya Fedulova V. M. Gorbatov Federal Research Center for Food Systems of RAS, Experimental-clinical research laboratory of bioactive substances of animal origin, Talalikhina st., 26, 109316, Moscow, Russia, Tel.: +74956769211



two-dimensional electrophoresis, muscle protein, isoelectric focusing, meat


It is important to understand the molecular mechanisms that take place in muscle tissues and to predict meat quality characteristics. One of the most popular methods is two-dimensional electrophoresis, which allows us to visualize, share and identify different molecules, including meat proteins. However, the standard conditions of this method are not universal for all types of raw material, so the authors suggest a new variation of two-dimensional electrophoresis for muscle tissue analysis. Samples were tested by the classical version of isoelectric focusing (cathode buffer in the top and anode buffer in the bottom chamber of the electrophoresis cell) and its variation (anode buffer in the top and cathode buffer in the bottom chamber of the electrophoresis cell). Next, extruded gels were incubated in two different buffer systems: the first was equilibration buffer I (6 M urea, 20% w/v glycerol, 2% w/v SDS and 1% w/v Ditiothreitol in 375 mM Tris-HCl buffer, pH 8.8) followed by equilibration buffer II (6 M urea, 20% w/v glycerol, 2% w/v SDS and 4% w/v iodoacetamide in 375 mM Tris-HCl buffer pH 8.8 and the second, buffer А, consisting of 5 M urea, 2% w/v SDS, 5% v/v mercaptoethanol, 62.5 mM Tris-HCl buffer, pH 6.8 and 0.01% w/v bromophenol blue. Electrophoretic studies of muscle tissue revealed the best protein separation after changing the direction of the current (authors' variation), while no differences were detected after changing incubation buffers.


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How to Cite

Akhremko, A., Vasilevskaya, E. R., & Fedulova, L. (2020). Adaptation of two-dimensional electrophoresis for muscle tissue analysis. Potravinarstvo Slovak Journal of Food Sciences, 14, 595–601.