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Monitoring recombinant protein expression in bacteria by rapid evaporative ionisation mass spectrometry
Rationale There is increasing interest in methods of direct analysis mass spectrometry that bypass complex sample preparation steps. Methods One of the most interesting new ionisation methods is rapid evaporative ionisation mass spectrometry (REIMS) in which samples are vapourised and the combustion...
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Published in: | Rapid communications in mass spectrometry 2021-04, Vol.35 (S2), p.e8670-n/a |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Rationale
There is increasing interest in methods of direct analysis mass spectrometry that bypass complex sample preparation steps.
Methods
One of the most interesting new ionisation methods is rapid evaporative ionisation mass spectrometry (REIMS) in which samples are vapourised and the combustion products are subsequently ionised and analysed by mass spectrometry (Synapt G2si). The only sample preparation required is the recovery of a cell pellet from a culture that can be analysed immediately.
Results
We demonstrate that REIMS can be used to monitor the expression of heterologous recombinant proteins in Escherichia coli. Clear segregation was achievable between bacteria harvesting plasmids that were strongly expressed and other cultures in which the plasmid did not result in the expression of large amounts of recombinant product.
Conclusions
REIMS has considerable potential as a nearāinstantaneous monitoring tool for protein production in a biotechnology environment. |
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ISSN: | 0951-4198 1097-0231 |
DOI: | 10.1002/rcm.8670 |