1998
DOI: 10.1002/(sici)1097-0290(19980820)59:4<461::aid-bit9>3.0.co;2-e
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Contribution of protein charge to partitioning in aqueous two-phase systems

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Cited by 24 publications
(22 citation statements)
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“…It has been well established that in aqueous biphase systems, coulombic forces can be an important factor in determining the partitioning of biomaterials, especially charged particles [2,37,38]. Walter and Selby [37] found that introducing a positively charged polymer into the PEG/dextran biphase system greatly enhanced the yield of negatively charged dog red blood cells in the phase in which the charged polymer predominated.…”
Section: Introductionmentioning
confidence: 99%
“…It has been well established that in aqueous biphase systems, coulombic forces can be an important factor in determining the partitioning of biomaterials, especially charged particles [2,37,38]. Walter and Selby [37] found that introducing a positively charged polymer into the PEG/dextran biphase system greatly enhanced the yield of negatively charged dog red blood cells in the phase in which the charged polymer predominated.…”
Section: Introductionmentioning
confidence: 99%
“…These findings will improve the knowledge base for a wide range of emerging fields like refolding in a phase system (Forciniti, 1994;Spears et al, 1995) or the construction of fusion tags to enhance partitioning (Berggren et al, 1999;Malmsten et al, 1998). Further investigations on charge-modified T4-lysozymes (Luther et al, 1994(Luther et al, , 1995Fan et al, 1998) will give us more insight into the so-called "electrostatic potential" of these systems (Grossman et al, 1997(Grossman et al, , 1998Tintinger et al, 1997aTintinger et al, , 1997b. The latter is currently being investigated in collaboration with the research group of Prof. G. Maurer (Univ.…”
Section: Resultsmentioning
confidence: 98%
“…Properties of T4-lysozyme mutants (Dao Pin et al, 1991;Matthews, 1995 (Cleland et al, 1990(Cleland et al, , 1992Laliberté et al, 1994, Maeda et al, 1995Tams et al, 1996). For the experiments we choose very well-described proteins, the wildtype (WT) and the cysteine free WT*, L99A and V149T mutants of T4-lysozyme (Fan et al, 1998;Matthews et al, 1995). L99A and V149T have an additional mutation in the protein core and are markedly less stable compared to the WT and WT* enzyme against thermal denaturation (Table I).…”
Section: Stability Investigationsmentioning
confidence: 99%
“…Factors and mechanisms that cause the distribution of biomolecules over the different phases are poorly understood. The value of the overall distribution coefficient depends on the molecular size [32], charge [33][34][35][36], hydrophobicity [37][38][39], solubility and affinity [40]. However, not all these parameters are equally important, this depends on the chosen system.…”
Section: Liquid-liquid Extractionmentioning
confidence: 99%