Figure 2
From: Seed storage proteins of the globulin family are cleaved post-translationally in wheat embryos
Globulin diversity is greater in the embryo-enriched fraction than in the endosperm as observed by 2-dimensional electrophoresis. Salt-soluble globulins were extracted from AC Barrie wheat seed endosperm (panels a, b) and embryo-enriched (panels c, d, e) fractions and separated by 2-DE. Proteins were stained with CBB R-250 (panels a, c) or transferred to nitrocellulose and probed with polyclonal rabbit anti-Glo-3A antiserum (panels b, d, e). Marker lanes (M) are Pre-stained Benchmark (Invitrogen). Molecular masses shown on immunoblots are approximations. Spots chosen for mass spectrometry are labeled 1–5 and marked with arrows, and represent a sampling of the major observed molecular masses ( ~30 kDa and ~50 kDa) with isoelectric points in the acidic (pH 3), neutral (pH 6–7) and basic (pH 9–10) regions. Circled spots are non-specific spots common to blots probed with pre-immune serum and anti-Glo-3A antibodies.