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Several CSF-restricted IgGλ bands in this sample were clearly visible in all four runs.
No cross-reactivity of the serum IgGκ paraprotein was seen on the membrane tested for IgGλ; several free κ bands in this sample had different migration positions than IgGκ bands.
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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.
Except the band at 1470 cm−1, all ammonium bands in the sample spectrum are also present in the spectrum of aluminium ammonium sulfate dodecahydrate (ammonium alum, NH4Al SO4 2·12H2O) [32].
Telomere shortening was quantified by determining the percentage of telomere bands less than 1.4 kb to the total number of bands in the sample.
Telomere shortening was quantified by determining the percentage of telomere bands less than 1.0 kb to the total number of bands in the sample.
We did not find any D band at 1,354 cm−1 in this sample showing that there is no disorder in the aromatic network structure of the dopant C.
At the cell surface, the band profile of wild-type P2X2 was somewhat altered; it appeared that a greater proportion of uppermost band was present in this 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).
The bands observed for this sample in the 350 390 nm region including CEs at 386, 375, and 359 nm, suggested other heme species (e.g., heme dimer) may be bound, causing conformational distortion within certain protein cavities.
The presence of single bands in each sample was subsequently confirmed using DNA gel electrophoresis.
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