muramidase has been researched along with pentaethylene-glycol-monododecyl-ether* in 1 studies
1 other study(ies) available for muramidase and pentaethylene-glycol-monododecyl-ether
Article | Year |
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Protein partitioning in weakly charged polymer-surfactant aqueous two-phase systems.
The study includes partitioning of proteins in aqueous two-phase systems consisting of the polymer dextran and the non-ionic surfactant C12E5 (pentaethylene glycol mono-n-dodecyl ether). In this system a micelle-enriched phase is in equilibrium with a polymer-enriched phase. Charges can be introduced into the micelles by the addition of charged surfactants. The charge of the mixed micelles is easily varied in sign and magnitude independently of pH, by the addition of different amounts of negatively charged surfactant, sodium dodecyl sulphate (SDS), or positively charged surfactant dodecyl trimethyl ammonium chloride (DoTAC). A series of water-soluble model proteins (BSA, beta-lactoglobulin, myoglobin, cytochrome c and lysozyme), with different net charges at pH 7.1, have been partitioned in non-charged systems and in systems with charged mixed micelles or charged polymer (dextran sulphate). It is shown that partition coefficients for charged proteins in dextran-C12E5 systems can be strongly affected by addition of charged surfactants (SDS, DoTAC) or polymer (dextran sulphate) and that the effects are directly correlated to protein net charge. Topics: Buffers; Cytochrome c Group; Dextran Sulfate; Ethers; Hydrogen-Ion Concentration; Isoelectric Point; Lactoglobulins; Micelles; Muramidase; Myoglobin; Polyethylene Glycols; Polymers; Proteins; Quaternary Ammonium Compounds; Serum Albumin, Bovine; Sodium Chloride; Sodium Dodecyl Sulfate; Surface Properties; Surface-Active Agents; Water | 1996 |