Disulfide-linked peptides in the chloroplast thylakoid membrane.
Two peptides move out from the diagonal when dodecyl sulfate gels of pea leaf chloroplast thylakoid membrane proteins are treated with a reducing agent and electrophoresed in the second dimension. Apparently two of the proteins in the thylakoid membrane are disulfide linked dimers. Additional changes in the electrophoretic mobility of certian peptides occur when thylakoid membranes are denatured in the presence of reducing agents: these peptides probably contain intrapeptide disulfide bonds or prosthetic groups covalently attached to the peptide through disulfide bonds.
D002736:Chloroplasts / Q000032:analysis*; D004220:Disulfides / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D007425:Intracellular Membranes / Q000032:analysis; D008565:Membrane Proteins / Q000032:analysis*; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis*; D010940:Plant Proteins / Q000032:analysis*
D004220:Disulfides; D008565:Membrane Proteins; D010455:Peptides; D010940:Plant Proteins