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Within the amount of protein loaded on the gel, we detected only a single band in each sample running with the molecular mass corresponding to TBC1D4-short and TBC1D4-long.
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The presence of single bands in each sample was subsequently confirmed using DNA gel electrophoresis.
Proteins of different molecular weights were visualized as bands in each sample.
SDS-PAGE analysis of IS and AS protein-rich fractions revealed that the major bands in each sample were not the same (Fig. 3).
The corresponding functional groups (Ibarra et al. 1996; Maity and Mukherjee 2006) of the bands present in each sample are tabulated in Table 4.
Accordingly, the values of hyperphospho-BicD were normalized to the sum of both BicD bands in each individual sample.
It is found that there are three bands for each sample in the FT-IR spectra (Fig. 3).
Furthermore, replicate experiments resulted in comparable band intensities for each sample.
To normalise the total protein quantity in each sample, the band intensity of cyclin D-type proteins was divided by the band intensity of β-actin in the same sample.
The optical density (OD) values obtained from each band were normalized against the OD obtained from the L32 band in that sample by the following expression: (OD of the sample band / OD of the L32 band X 100).
In sample X5 a sulfate band was identified at 973 cm−1, which is consistent with the chromate stretching band in this sample being shifted to 846 cm−1.
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