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. 2004 Nov;186(21):7456–7459. doi: 10.1128/JB.186.21.7456-7459.2004

FIG. 2.

FIG. 2.

Images of chemiluminescent Western blots showing in vivo dimerization of Aer constructs after a 10-min treatment with the oxidant copper phenanthroline. (A) Serial dilutions of wild-type Aer. Lane 1 is the 0-min control, and lanes 2 to 8 are 10-min time points diluted as follows: lanes 2 and 3, undiluted sample; lanes 4 and 5, twofold dilution; lanes 6 and 7, fourfold dilution; lane 8, eightfold dilution. Mw, molecular weight markers; M, monomeric form of Aer; F, a 37-kDa proteolytic fragment of full-length Aer; M-M, dimerization between monomeric Aer proteins; M-F, dimerization between Aer monomer and proteolytic fragment. (B) Lanes: 1 and 2, wild-type Aer at 0 and 10 min; 3 and 4, control without cysteines (Aer-C193S/C203A/C253A) at 0 and 10 min; 5 and 6, Aer-C193 (Aer-C203A/C253A) at 0 and 10 min; 7 and 8, Aer-C203 (Aer-C193S/C253A) at 0 and 10 min; 9 and 10, Aer-C253 (Aer-C193S/C203A) at 0 and 10 min; 11 and 12, His6x-Aer2-285 at 0 and 10 min; 13 and 14, His6x-Aer2-231 at 0 and 10 min.