Combined 2D electrophoretic approaches for the study of white lupin mature seed storage proteome

In this work, a combination of two experimental approaches to identify the main protein components of white lupin seed (Lupinus albus, L.) have been used. One is the canonical proteomic approach including 2D electrophoretic separation and mass spectrometry; the other approach is a group comparative 2D electrophoretic analysis of cotyledonary protein families. To this second purpose, the three main families of lupin seed proteins, namely α-conglutins, the 11S globulin fraction, β-conglutins, the 7S globulin fraction, and γ-conglutin, a basic 7S protein, were isolated by conventional biochemical techniques and their 2D reference maps were compared with the total protein map.