Sentence examples for pooling of fractions from inspiring English sources

Arrows indicate the pooling of fractions which leads to pure compounds.

While this pooling of fractions from sucrose gradients precludes drawing conclusions on the regulation of translation elongation or termination, it allows analyzing translational regulation at the step of translation initiation.

A total of 58 fractions were obtained from CDEb5 after Sephadex LH-20 chromatography, but after pooling of fractions that presented similar compound profiles across the TLC plates (data not shown), six different fractions were obtained (CDEb5-1 to CDEb5-6), ranging from 2.8 to 188.4 mg in yield, or 0.36 24.28% of the CDEb5 fraction and 0 0.04% of the initial bee pollen (Table 5).

A selected pool of fractions containing DNA in the 0.7 1.5 kb size range, were subjected to digestion with λ-exonuclease, and the resulting DNA constituted our test DNA.

Pools of fractions 3 5 (enriched in lipid rafts) and fractions 10 12 (largely deficient in lipid rafts) from these sucrose gradients led to the raft and non-raft fractions, respectively, which were subsequently subjected to Western blotting.

Both pools of fractions were immunoprecipitated for DQ (Fig. 7, lanes 1 and 2) and for DR (lanes 3 and 4) and subsequently immunoblotted for DRα (upper panels) or for DQβ or DRβ chains (lower panels).

To 100 µl of a pool of fractions 7 and 8 or of fractions 14 and 15 of the sucrose gradient (without Tris) separated Raji cell lysates increasing amounts of the thiol- cleavable crosslinker 3,3'-dithiobis [succinimidyl propionate] (DSP) were added.

RNA was extracted from pools of fractions containing either unbound snoRNAs or pre-ribosomal complexes and processed as shown in Fig 1A.

Thus the PM pool of fractions 15-20 from the gradient was subjected to 2PAP, and analyzed as before except that we switched to high sensitivity chemiluminescence substrates with 100-1000 theesensitivitytivity of the previous analyses to assess ER and mitochondrial contamination.

The lower reproducibility mostly results from the fractionation of peptides prior to LC-MS/MS analysis, and the subsequent pooling of eluted fractions, which can result in unequal/uncontrolled pooling, as was the case in the present study.

The soluble protein fraction was obtained by incubating resuspended cell pellets in 40 µl B-PER (PIERCE) containing 10 µg/ml DNase I for 10 min. at room temperature followed by centrifugation at 20,000 g for 12 min. The supernatant was transferred to a fresh tube and the pellet re-extracted as above followed by pooling of supernatant fractions.