For analysis of proteins, polyacrylamide gel electrophoresis is a widely used technique, to separate proteins according to their electrophoretic mobility. Two dimensional gel electrophoresis (2-DE), described by O'Farrel, represents one of the most appropriate techniques for separation of complex protein patterns, and combines IEF in the first dimension, so proteins are separated according to pI and separation due to the moleclar weight in the second dimension. Due to the capability a lot of possibilities were established for plant proteomic analysis.
However, to obtain high quality resolution of proteins in proteomic analysis, sample preparation is important for optimal results. Plant tissue is often rich in compounds that interfere with 2-DE e.g. phenolic compounds and natural rubber. Most of the difficulties in plant proteomics are associated with co- extraction of non- protein components, which affect separation of proteins and causes to protein loss.
In our investigation we explored an approach to separate proteins from latices of genus Euphorbia L. in particular by 2-DE, to elucidate the complex composition of containing proteins. Different protein patterns were analyzed, and compared by software analysis based on the corresponded number of spots. Comparative analysis exhibited different protein patterns and allowed the conclusion of the occurence of individual protein patterns of different species.
References:
[1] O'Farell PH. High resolution two- dimensional electrophoresis of proteins. J Biol Chem 1975; 250: 4007 – 21
[2] Wang W. Optimizing protein extraction from plant tissues for enhanced proteomics analysis. J Sep Science 2008; 31: 2032 – 2039
[3] Wahler D. Proteomic analysis of latex from the rubber-producing plant Taraxacum brevicorniculatum. Proteomics 2012; 12: 901 – 905
