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Exact(16)
A single large pool was used in each fractionation experiment to ensure that fractions were identical between behavioural replicates and biochemical analyses.
The residue from each fractionation step was used to obtain the subsequent fraction.
Figure 2 summarizes the total number of phosphopeptides, the number of unique phosphopeptides obtained from each fractionation approach, and the distribution of phosphopeptides in different fractions.
Each fractionation was then immunoblotted.
For each fractionation approach, the number of peptides, proteins, and protein groups identified by 1 (95% and 99% confidence), 2, and >2 (95% confidence) peptides are reported in Table 1.
The extracts from each fractionation step were evaporated to dryness under vacuum.
Similar(44)
SDS-PAGE analysis of each fraction revealed that fractionation enriched some of the minor proteins by placing majority of the albumin into a single fraction).
To test this possibility, we profiled primary metabolites in above ground tissues of 4-week-old plants of each genotype (GKO and WT, N = 5 plants each) by fractionation and gas chromatography mass spectrometry (GC-MS).
Since the RNA from each length fractionation was electrophoresed for a slightly different period of time, the slices from each gel occur at different distances from the well and represent different ranges of RNA length.
In order to compare the length profiles for a given gene generated from each length fractionation, it was necessary to scale the data for two of the length fractionations along the gel mobility axis so that they correspond to the data from the third length fractionation.
In order to minimize such errors, prior to each RP fractionation, a standard solution (known RT and log Kow) was injected to the preparative LC column to check the stability of the system.
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