Production of Human Cu,Zn SOD with Higher Activity and Lower Toxicity in<i> E. coli</i> via Mutation of Free Cysteine Residues

<div>Effects of cysteine mutations on the solubility of hSOD1 expressed in<i> E. coli</i>. (a) SDS-PAGE of soluble and insoluble protein fractions. (b) Western blotting of soluble proteins. Proteins on the SDS-PAGE gel were transferred to membranes, blotted with an anti-SOD1 antibody to determine the relative percentage of the soluble fractions. The lanes contain wtSOD1 or three mutants as indicated. (c) Histogram of the distribution of the soluble fractions of SOD1 in<i> E. coli</i> as determined by 4 independent Western blot experiments.</div>

BioMed Research International

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Figure 2

Figure 2: Production of Human Cu,Zn SOD with Higher Activity and Lower Toxicity in<i> E. coli</i> via Mutation of Free Cysteine Residues 

BioMed Research International

Production of Human Cu,Zn SOD with Higher Activity and Lower Toxicity in E. coli via Mutation of Free Cysteine Residues

Figure 2