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Peptide sequences appear 1.3 times redundant per up-regulated protein on average in the peptide profile matrix, and do not seem always up-regulated due to tailing in LC retention time (40%), modifications (40%) and mass determination errors (20%).
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Based on MS2 fragmentation patterns and exact mass determination (4-digit mass errors of < 1.6 ppm), these peaks were annotated as desulfoBGLS (dBGLS) and malonylated dBGLS (mdBGLS).
Therefore, it was also included for mass determination.
The sample (5 μL) was used for molecular mass determination using an ESI Q-TOF mass spectrometer (Micromass, Manchester, England).
The sample (5 μL) was used for molecular mass determination using an MALDI-TOF mass spectrometer (JMS-S3000, Japan).
The sample (5 μL) was used for molecular mass determination using JOEL MALDI-TOF.
Native mass determination was carried out by ESI-MS analysis.
Eluted proteins were infused into a Waters Q-Tof II™ mass spectrometer for mass determination.
The purified protein was subjected to MALDI-MS analysis for molecular mass determination.
These sex determination errors are attributable to erroneous genotypes.
Fully expanded leaves were counted before dry mass determination.
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CEO of Professional Science Editing for Scientists @ prosciediting.com