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 |
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| Authors: | R.H.P. Law H.C. Robinson M.J. Rowley I.R. Mackay |
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| Affiliation: | (1) Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, 3800, Australia |
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| 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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| Keywords: | alcohol dehydrogenase glutamic acid decarboxylase immobilised metal affinity chromatography methyl formate Pichia |
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