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Abstract for Thioredoxin, E. coli, Recombinant
Thioredoxin is a low molecular weight oxidoreductase that contains a single
disulfide active site. It was originally isolated from E. coli as a
hydrogen donor for ribonucleotide reductase, although thioredoxins from plants
and mammals also have been characterized. The only known physiological roles for
thioredoxins are in the assembly of filamentous phage and as an accessory
protein for phage T7 DNA polymerase. Multiple in vitro substrates, however, have
been shown for thio-redoxin including insulin, coagulation factors, proteolytic
enzymes and the glucocorticoid receptor. It has been suggested that thioredoxin
may catalyze the formation of correct disulfides during protein folding because
of its ability to act as an efficient oxidoreductant. This could be especially
useful in refolding proteins expressed in E. coli, which have a
tendency to fold improperly. To this end, thioredoxin has been shown to act as a
protein disulfide isomerase, catalyzing the formation and rearrangement of
protein disulfide bonds in ribonuclease.
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