Anomalous behaviour of sodium in isotachophoresis

J.C. Reijenga; T.P.E.M. Verheggen

doi:10.1016/S0021-9673%2801%2988741-0

Anomalous behaviour of sodium in isotachophoresis

J.C. Reijenga, T.P.E.M. Verheggen

Chemical Engineering and Chemistry

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Abstract

Using a cationic operational system in capillary isotachophoresis, millimolar concentrations of sodium were determined in the absence and presence of serum proteins. With several internal standards, the reproducibility of the sodium determination was significantly poorer in the presence of proteins, even after partial thermal degradation. The results are explained by protein—sodium interaction in the injection port, where the electric field strength was sixteen times lower than in the separation capillary.

Original language	English
Pages (from-to)	471-474
Journal	Journal of Chromatography, A
Volume	545
Issue number	2
DOIs	https://doi.org/10.1016/S0021-9673%2801%2988741-0 https://doi.org/10.1016/S0021-9673(01)88741-0
Publication status	Published - 1991

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title = "Anomalous behaviour of sodium in isotachophoresis",

abstract = "Using a cationic operational system in capillary isotachophoresis, millimolar concentrations of sodium were determined in the absence and presence of serum proteins. With several internal standards, the reproducibility of the sodium determination was significantly poorer in the presence of proteins, even after partial thermal degradation. The results are explained by protein—sodium interaction in the injection port, where the electric field strength was sixteen times lower than in the separation capillary.",

author = "J.C. Reijenga and T.P.E.M. Verheggen",

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T1 - Anomalous behaviour of sodium in isotachophoresis

AU - Reijenga, J.C.

AU - Verheggen, T.P.E.M.

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Y1 - 1991

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AB - Using a cationic operational system in capillary isotachophoresis, millimolar concentrations of sodium were determined in the absence and presence of serum proteins. With several internal standards, the reproducibility of the sodium determination was significantly poorer in the presence of proteins, even after partial thermal degradation. The results are explained by protein—sodium interaction in the injection port, where the electric field strength was sixteen times lower than in the separation capillary.

U2 - 10.1016/S0021-9673%2801%2988741-0

DO - 10.1016/S0021-9673%2801%2988741-0

M3 - Article

VL - 545

SP - 471

EP - 474

JO - Journal of Chromatography, A

JF - Journal of Chromatography, A

SN - 0021-9673

IS - 2

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