Heterotypic aggregation of an in vitro synthesised low-molecular-weight glutenin subunit. (Contributo in atti di convegno)

Type
Label
  • Heterotypic aggregation of an in vitro synthesised low-molecular-weight glutenin subunit. (Contributo in atti di convegno) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Alternative label
  • Orsi, A., Sparvoli, F., Della Cristina, P.A., and Ceriotti A. (2003)
    Heterotypic aggregation of an in vitro synthesised low-molecular-weight glutenin subunit.
    in 8th Gluten Workshop, Viterbo
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Orsi, A., Sparvoli, F., Della Cristina, P.A., and Ceriotti A. (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note
  • Editore: The Royal Society of Chemistry, pp 26-29 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
  • We have previously described an in vitro system based on plant components that allows the synthesis, translocation and folding of a low-molecular-weight glutenin subunit (LMW-GS). The system is composed of a wheat germ extract supplemented with microsomal membranes isolated from developing bean cotyledons.LMW-GS are characterized by the presence of three conserved intrachain disulfide bonds. We previously found that when in vitro synthesized mRNA coding for the B11-33 LMW-GS4 is translated in the presence of sufficient levels of oxidized glutathione (GSSG), the protein accumulates as a monomer containing intrachain disulfide bonds. Conversely, when translation is performed under reducing conditions the in vitro synthesized protein misfolds and enters high molecular weight aggregates. Here we present a further characterization of the aggregates formed in this in vitro system (literal)
Titolo
  • Heterotypic aggregation of an in vitro synthesised low-molecular-weight glutenin subunit. (literal)
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