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(2) Protein partitioning between coexisting membrane phases.
Lorent JH, Levental I. Structural determinants of protein partitioning into ordered membrane domains and lipid rafts.
Pujar, N. S. & Zydney, A. L. Electrostatic effects on protein partitioning in size-exclusion chromatography and membrane ultrafiltration.
Protein partitioning kinetics were generally similar at volume ratios (Vr = Vaq/Vrm) of Vr = 1 and Vr = 5.
Among various factors, polymer concentration and polymer molecular weight are essential and have strong impact on the protein partitioning in these systems.
The kinetics of protein partitioning have been determined for the batch extraction of proteins using reverse micellar phases comprised of AOT in isooctane.
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The protein partition could almost quantitatively be predicted from the peptide partition data.
In general, protein partition coefficients ranged from 0 to 10 in buffers on 0.1 M ionic strength.
Both biomass and recombinant protein partitioned to the bottom phase during extractive bioconversion.
This represents a 1322-fold increase in the protein partition coefficient in comparison to the non-PEGylated protein (Kc = 0.013).
Specific activity, activity recovery, purification fold, volume ratio, enzyme and protein partition coefficients were considered as response variables.
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