%0 Figure %A Goyal, Pankaj %A Pandey, Dharmendra %A Brünnert, Daniela %A Hammer, Elke %A Zygmunt, Marek %A Siess, Wolfgang %D 2013 %T Endogenous and recombinant human His-cofilin has an intracellular disulphide bond. %U https://plos.figshare.com/articles/figure/_Endogenous_and_recombinant_human_His_cofilin_has_an_intracellular_disulphide_bond_/767779 %R 10.1371/journal.pone.0071769.g002 %2 https://plos.figshare.com/ndownloader/files/1147363 %K biophysics %K Cell motility %K Actin filaments %K Molecular cell biology %K Cellular types %K Endothelial cells %K Signal transduction %K Signaling in cellular processes %K Thrombin signaling %K gene expression %K recombinant %K his-cofilin %K intracellular %K disulphide %X

A) Recombinant human His-cofilin, platelet, and endothelial cell lysates were subjected to SDS-PAGE under reducing (with ß-mercapto-ethanol; +ßM) and non-reducing conditions (without ß-mercapto-ethanol; -ßM) and then immunoblotted with anti-cofilin antibody. Monomeric cofilin showed higher electrophoretic mobility under non-reducing conditions than under reducing conditions. Moreover, oligomers of different molecular masses of recombinant His-cofilin but not of endogenous cofilin were observed under non-reducing condition, suggesting the involvement of intermolecular disulphide bonding in in vitro oligomerization. B) Recombinant human cofilin (with and without His-tag) were subjected to SDS-PAGE under reducing and non-reducing conditions and analyzed by Coomassie blue staining. Both types of recombinant cofilin demonstrate a higher electrophoretic mobility under non-reducing conditions as compared to reducing conditions.

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