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. Author manuscript; available in PMC: 2012 Jun 10.
Published in final edited form as: Cytoskeleton (Hoboken). 2011 Jun 10;68(6):340–354. doi: 10.1002/cm.20516

Figure 5. Actin can spontaneously oxidize on C285 and C374 residues in vitro.

Figure 5

(A) act1C17,217Ap under non-reducing conditions (lane 1) runs as a doublet at ~42 KDa, whereas under reducing conditions (β-mercaptoethanol addition; lane 2) it runs as a single band that co-migrates with the upper band in the non-reducing sample. (B) Visualization of act1C17,217Ap separated on an 8% gel under non-reducing conditions shows higher molecular weight oligomers that indicate the formation of intermolecular disulfide bonds (see arrows) involving cysteine 285 and/or cysteine 374. The open arrowhead indicates intra-molecularly disulfide-bonded actin that was observed under these conditions.