Post-translational cleavage pattern of Lupinus angustifolius γ-conglutin.

The results indicate that the proteolytic processing of γ-conglutin signal peptide is not precise. On the other hand, the post-translational cleavage between α- and β-subunits of γ-conglutin is very conserved. Interestingly, the results also indicate that proteolytic processing leading to the formation of two subunits of γ-conglutin is incomplete, leaving a certain amount of the protein in an uncut form. © 2018 Society of Chemical Industry.