Disulphide bonds, recombinant

Recently, active recombinant a-LTX has been generated using bacteria in which both thioredoxin reductase and glutathione reductase are inactivated to improve the formation of disulphide bonds in expressed proteins (Li et al. 2005). The toxin is expressed as a fusion with glutathione-S-transferase (GST), which is used for affinity purification of the recombinant toxin and can be subsequently removed by selective proteolysis. Considering the relative ease of generating recombinant proteins in bacteria, this approach will facilitate structure-function studies of a-LTX. 

Raschdorf, F., Dahinden, R., Maerki, W., et al. (1988) Location of disulphide bonds in human insulin-like growth factors (IGFs) synthesized by recombinant DNA technology. Biomedical and Environmental Mass Spectrometry, 16,3-8. 

Oxidation of disulphides and thiolsulphinates with excess N2O4 gives mixtures of thiolsulphonates, indicating S—S bond cleavage into sulphenyl and sulphinyl nitrites and nitrates, followed by recombination. ... 

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