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The polymerisations have been monitored as a function of monomer conversion and the polymer prepared at high conversion has been fractionated across the molecular weight distribution.
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We were able to identify and quantify relative amounts of ~4,750 non-redundant proteins by studying 200 subproteomes (10 fractions at the protein level, with each protein fraction further fractionated into 20 peptide-level subproteomes) across four different cell types (results to be published).
The polymers were fractionated by fractional precipitation.
Active fractions were further fractionated and assayed.
CSF peptides were fractionated into 30 fractions.
The gradient was then fractionated into 12 fractions [ 13].
Fraction S14 was further fractionated by RP-HPLC.
We fractionated mouse 3T3 soluble chromatin across isokinetic 6 40% sucrose gradients and precipitated the protein from each fraction and blotted for endogenous Lsh (sedimentation of open and compacted chromatin was confirmed by gel electrophoresis)).
The gradients were fractionated into 38 1-mL fractions.
Briefly, cell lysates were fractionated as nuclear and cytoplasmic fractions.
Gradients were fractionated by a Piston Gradient Fractionator (BioComp).
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