原创力文档Eukaryotic Proteins Expressed in Escherichia coli = An Improved Thrombin Cleavage and Purification Procedure of Fusion Proteins with Glutathione S Transferase英文文献.pdfVIP
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ANALYTICAL BIOCHEMISTRY 192,262-267 (19%)
Eukaryotic Proteins Expressed in Escherichia co/i= An
Improved Thrombin Cleavage and Purification Procedure
of Fusion Proteins with Glutathione S-Transferase
KunLiang Guan and Jack E. Dixon
Department of Biochemistry and Walther Cancer Institute, Purdue University, West Lafayette, Indiana 47907
Received July 12, 1990
peptide and also plays a main role in the levels of ex-
Several systems have been developed to allow for pression which are attained. In general, the most serious
rapid and efficient purification of recombinant pro- problems encountered with recombinant proteins re-
teins expressed in bacteria. The expression of polypep- volve around their insolubility, aggregation, or incorrect
tides in frame with glutathione S-transferase (GST) al- folding (1). Even when moderate levels of recombinant
lows for purification of the fusion proteins from crude protein production in bacteria are attained, it can be
bacterial extracts under nondenaturing conditions by difficult to purify the recombinant proteins efficiently.
affinity chromatography on glutathione agarose (D. B. Several expression systems ha
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