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Sökning: L773:0021 9673 > Mälardalens universitet

  • Resultat 1-3 av 3
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1.
  • Berna, N, et al. (författare)
  • Polyol-promoted adsorption of serum proteins to amphiphilic agarose-based adsorbents
  • 1997
  • Ingår i: Journal of Chromatography A. - UNIV UPPSALA,BIOCHEM SEPARAT CTR,BMC,S-75123 UPPSALA,SWEDEN. MALARDALEN UNIV,DEPT CHEM ENGN,S-63105 ESKILSTUNA,SWEDEN. : ELSEVIER SCIENCE BV. - 0021-9673 .- 1873-3778. ; 764:2, s. 193-200
  • Tidskriftsartikel (refereegranskat)abstract
    • We tested the promotion of protein adsorption onto amphiphilic agarose-based adsorbents by addition of high concentrations of polyols during the adsorption phase. C-3- to C-5-polyols were inefficient in promoting protein adsorption, whereas some of the C-6-polyols studied (sorbitol, dulcitol and mannitol) could promote serum protein adsorption onto mercaptomethylene pyridine-derivatized agarose, octyl- and phenyl-Sepharose. Sorbitol was the most potent protein adsorption promoter, with a direct relation between the amount of protein adsorbed and the concentration of sorbitol. For each chromatographic gel, the effects of increasing concentrations of sorbitol or sodium sulfate on protein adsorption were similar and two-dimensional electrophoresis revealed the preservation of the protein adsorption specificity whether sorbitol or sodium sulfate was used. These results show that a water-structuring salt or a polyol can promote protein adsorption in the same manner, presumably by a related mechanism.
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2.
  • Oscarsson, Sven, et al. (författare)
  • Amphiphilic agarose-based adsorbents for chromatography comparative study of adsorption capacities and desorption efficiencies
  • 1995
  • Ingår i: Journal of Chromatography A. - : Elsevier BV. - 0021-9673 .- 1873-3778. ; 689:1, s. 3-12
  • Tidskriftsartikel (refereegranskat)abstract
    • A number of hydrophobic derivatives attached to cross-linked agarose were studied as protein adsorbents. Differences in the adsorption and desorption behaviour were determined as functions of type and concentration of selected salts. Whereas octyl- and phenyl-Sepharose adsorb serum albumin preferentially, pyridyl-S-agarose shows a much stronger preferential affinity for IgG in the presence of high concentrations of lyotropic salts, such as sulphates. In contrast to pyridyl-S-agarose, a large portion of proteins remained fixed to octyl- and phenyl-Sepharose after extensive washing with 1 M NaOH.
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3.
  • Oscarsson, Sven, et al. (författare)
  • Salt-promoted adsorption of proteins onto amphiphilic agarose-based adsorbents. II. Effects of salt and salt concentration
  • 1998
  • Ingår i: Journal of Chromatography A. - 0021-9673. ; 803:1-2, s. 83-93
  • Tidskriftsartikel (refereegranskat)abstract
    • The effects of different types of salts and salt concentrations on the selectivity in the adsorption of serum proteins have been compared for the amphiphilic agarose-based adsorbents Phenyl-Sepharose, Octyl-Sepharose, butyl-agarose and mercaptopyridine-derivatized agarose. By use of multivariate analysis, the complex interrelationships for the different combined effects were evaluated. From these analyses conclusions about similarities and/or dissimilarities in the mechanisms involved in adsorption of proteins on respective adsorbent were made.
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  • Resultat 1-3 av 3
Typ av publikation
tidskriftsartikel (3)
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refereegranskat (3)
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Oscarsson, Sven (3)
Berna, P (1)
Berna, N (1)
Chaga, Grigoriy (1)
Porath, Jerker (1)
Kårsnäs, Per (1)
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Angulo-Tatis, Dalila (1)
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Mälardalens universitet  (3)Ta bort avgränsningen
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Engelska (3)
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Naturvetenskap (3)

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