ISSN:
0173-0835
Keywords:
Capillary electrophoresis
;
Protein
;
Polymer solutions
;
Dextran
;
Sodium dodecyl sulfate
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Capillary electrophoresis in presence of sodium dodecyl sulfate (SDS) and 10% w/v of oligomeric dextran with molecular weight of just above 1000 was found to be an efficient medium for size-dependent separation of proteins (Karim, M. R., Janson, J.-C., Takagi, T., Electrophoresis 1994, 15, 1531-1534). The separations were found to be highly reproducible, both with respect to the position and relative amounts of the peaks. No evidence for a network structure in the medium could be found on examination of the effect of dextran concentration and viscosity measurements. The separation mechanism appears to be different from sieving by a polymer network structure. In free solution, SDS-protein complexes with molecular weights 〉 10000 migrate with almost the same mobilities, irrespective of their molecular weight (this behavior is called free draining). Such SDS-complexes of proteins or peptides with molecular weights 〈 10000, however, tend to increase their negatively signed mobilities with decreasing molecular weight (Karim, M. R., Shinagawa, S., Takagi, T., Electrophoresis 1994, 15, 1141-1146). Our working hypothesis is that in presence of the oligomeric dextran, the range of deviation from the free-draining electrophoretic behavior extends to higher molecular weights, resulting in a novel separation made.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/elps.11501601242
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