Abstract
We expressed a recombinant human glutamic acid decarboxylase (rhGAD) tagged with a hexa-histidine sequence in the Pichia pastoris cytosol. When rhGAD was purified from cell lysates by immobilised metal affinity chromatography, a 38 kDa contaminant protein was evident. This ubiquitous 38 kDa protein was as a yeast alcohol dehydrogenase isozyme that can bind strongly to nickel. Strategies for its removal are discussed.
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Law, R., Robinson, H., Rowley, M. et al. The ubiquitous 38 kDa contaminant in glutamic acid decarboxylase preparation from the cytosol of Pichia pastoris after immobilised metal ion affinity chromatography is an alcohol dehydrogenase. Biotechnology Letters 23, 697–703 (2001). https://doi.org/10.1023/A:1010368921034
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DOI: https://doi.org/10.1023/A:1010368921034