The legumin precursor from white lupin seed. Identity of the subunits, assembly and proteolysis.

@article{Duranti1992TheLP,
  title={The legumin precursor from white lupin seed. Identity of the subunits, assembly and proteolysis.},
  author={Marcello M Duranti and Nicoletta Guerrieri and Paolo Cerletti and Giuseppe Vecchio},
  journal={European journal of biochemistry},
  year={1992},
  volume={206 3},
  pages={941-7}
}
The precursors of the legumin-like storage protein from developing white lupin seeds (35 days after flowering) are trimers composed of protomers of M(r) 72,000 or 67,000. Some subunits of these oligomers contain processed precursor polypeptides, namely alpha polypeptides of either 52,000 or 44,000 linked through disulphide bonds to a beta polypeptide of 21,000, typical of the mature legumin. The prolegumin is glycosylated. Legumin oligomers purified from the same seeds are both trimers and… CONTINUE READING