1999
DOI: 10.1016/s0021-9673(99)00038-2
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Aqueous two-phase systems containing self-associating block copolymers

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Cited by 48 publications
(32 citation statements)
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“…The incompatibility between EOPOEO and polysaccharides (e.g. dextran) can lead to the formation of ATPS (Svensson, Berggren, Veide, & Tjerneld, 1999;Tada, Loh, & Pessôa-Filho, 2004), that is to say, EOPOEO and polysaccharides would enrich in the opposite phases. As for the EOPOEO-salt ATPS, with increasing salt concentration, the polymer concentration in the top phase and the salt concentration in the bottom would increase (Haraguchi, Mohamed, & Loh, 2004).…”
Section: Effect Of Salt Concentrationmentioning
confidence: 99%
“…The incompatibility between EOPOEO and polysaccharides (e.g. dextran) can lead to the formation of ATPS (Svensson, Berggren, Veide, & Tjerneld, 1999;Tada, Loh, & Pessôa-Filho, 2004), that is to say, EOPOEO and polysaccharides would enrich in the opposite phases. As for the EOPOEO-salt ATPS, with increasing salt concentration, the polymer concentration in the top phase and the salt concentration in the bottom would increase (Haraguchi, Mohamed, & Loh, 2004).…”
Section: Effect Of Salt Concentrationmentioning
confidence: 99%
“…Moreover, there is a remarkable change in the phase diagrams when temperature is raised from 5 to 40 • C, which was ascribed to changes on the aggregation state of the copolymer molecules. Further work by the same group was reported by Svensson et al [12], who investigated the partitioning behavior of aminoacids, dipeptides and tripeptides in ATPS formed by dextran T500 and the block copolymer P105, and by Svensson et al [13], who determined the partition coefficients of some proteins in ATPS formed by dextran T500 and either F68 or P105.…”
Section: Introductionmentioning
confidence: 79%
“…Since pIs (isoelectric points) for TRY and LYS are 10.4 and 11.0, respectively [13], both proteins are positively charged in all the pHs assayed. Fig.…”
Section: Try and Lysmentioning
confidence: 99%
“…2 shows the BSA partitioning behaviour in the different buffer media, according to Table 1. K r values lower [13], therefore it will be positively charged at a pH lower than pI and negatively charged at a pH higher than pI.…”
Section: The Effects Of Salts and Ph On Protein Partitioningmentioning
confidence: 99%
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