In:
ELECTROPHORESIS, Wiley, Vol. 27, No. 14 ( 2006-07), p. 2933-2939
Kurzfassung:
MEKC of standard proteins was investigated on PDMS microfluidic devices. Standard proteins were labeled with AlexaFluor® 488 carboxylic acid tetrafluorophenyl ester and filtered through a size‐exclusion column to remove any small peptides and unreacted label. High‐efficiency MEKC separations of these standard proteins were performed using a buffer consisting of 10 mM sodium tetraborate, 25 mM SDS, and 20% v/v ACN. A separation of BSA using this buffer in a 3.0 cm long channel generated a peak with a plate height of 0.38 μm in 〈 20 s. Additional fast separations of myoglobin, α‐lactalbumin, lysozyme, and cytochrome c also yielded peaks with plate heights ranging from 0.54 to 0.72 μm. All proteins migrated with respect to their individual p I s. To improve the separations, we used a PDMS serpentine chip with tapered turns and a separation distance of 25 cm. The number of plates generated increased linearly with increasing separation distance on the extended separation channel chips; however, the resolution reached an asymptotic value after about 7 cm. This limited the peak capacity of the separation technique to 10–12.
Materialart:
Online-Ressource
ISSN:
0173-0835
,
1522-2683
DOI:
10.1002/elps.200500795
Sprache:
Englisch
Verlag:
Wiley
Publikationsdatum:
2006
ZDB Id:
1475486-1
SSG:
12
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