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- Title
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.
- Authors
Law, R. H. P.; Robinson, H. C.; Rowley, M. J.; Mackay, I. R.
- 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.
- Subjects
ALCOHOL dehydrogenase; GLUTAMIC acid; GLUTAMATE decarboxylase; PICHIA pastoris; CHROMATOGRAPHIC analysis; METAL ions
- Publication
Biotechnology Letters, 2001, Vol 23, Issue 9, p697
- ISSN
0141-5492
- Publication type
Article
- DOI
10.1023/A:1010368921034