A Study of Deproteinization Methods for Subsequent Serum Analysis with Capillary Electrophoresis

✍ Scribed by Pamela B. Ralston; Timothy G. Strein

• Publisher: Elsevier Science
• Year: 1997
• Tongue: English
• Weight: 116 KB
• Volume: 55
• Category: Article
• ISSN: 0026-265X
• DOI: 10.1006/mchj.1996.1421

✦ Synopsis

Fifteen different methods of serum protein removal are examined for applicability with subsequent serum analysis for low molecular mass metabolites and pharmaceutical agents by capillary electrophoresis (CE). Each of the deproteinization methods considered here has been reported in the literature and successfully used for serum protein removal in other applications. Two of the methods are found to be superior to the others for CE analysis. Protein removal by ultrafiltration with Centrifree Micropartition System filters and by precipitation using acetonitrile worked well for protein removal, as evidenced by reproducible (RSD õ6%) determinations of several low molecular weight components. The former is capable of analyzing for free metabolites only, while the latter was found to be somewhat problematic with respect to evaporation of the acetonitrile, causing potential problems with reproducibility. Both techniques for protein removal were clearly suitable for the subsequent serum analysis by CE in untreated fused silica capillaries.