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Abstract
<p class="first" id="d9120341e61">Plasmid expression vectors have been constructed
that direct the synthesis of foreign
polypeptides in Escherichia coli as fusions with the C terminus of Sj26, a 26-kDa
glutathione S-transferase (GST; EC 2.5.1.18) encoded by the parasitic helminth Schistosoma
japonicum. In the majority of cases, fusion proteins are soluble in aqueous solutions
and can be purified from crude bacterial lysates under non-denaturing conditions by
affinity chromatography on immobilised glutathione. Using batch wash procedures several
fusion proteins can be purified in parallel in under 2 h with yields of up to 15 micrograms
protein/ml of culture. The vectors have been engineered so that the GST carrier can
be cleaved from fusion proteins by digestion with site-specific proteases such as
thrombin or blood coagulation factor Xa, following which, the carrier and any uncleaved
fusion protein can be removed by absorption on glutathione-agarose. This system has
been used successfully for the expression and purification of more than 30 different
eukaryotic polypeptides.
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